FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2032961490> ?p ?o ?g. }

• W2032961490 endingPage "18960" @default.
• W2032961490 startingPage "18954" @default.
• W2032961490 abstract "Fibronectin is an extracellular matrix glycoprotein encoded by a single gene. Alternative RNA splicing has been reported at three sites, ED (extra type III domain)-A, ED-B, and the variable or V region. Articular cartilage fibronectin monomers are rarely (ED-A)+, but approximately 25% are (ED-B)+. RNA gel electrophoresis and Northern blot analysis identified two (ED-B)+ and two (ED-B)− fibronectin transcripts in cartilage, each pair differing by ~750 bases. This difference results from a previously unreported RNA splicing pattern that eliminates not only the V region but also nucleotides encoding protein segments III-15 and I-10. This new splice variant, which we designate (V+C)−, represents the majority of fibronectin transcripts in equine, canine, and rabbit articular cartilage but is absent in the liver. Reverse transcriptase-polymerase chain reaction analyses of 11 additional equine tissues failed to detect the (V+C)− splice variant, except for very low levels in lymph node, bone, aorta, and skin. Furthermore, chondrocytes grown in monolayer culture maintain high levels of fibronectin expression but stop expressing (V+C)− transcripts over time. The tissue-specific expression pattern of this novel fibronectin isoform suggests that it may have an important function in the matrix organization of cartilage. Fibronectin is an extracellular matrix glycoprotein encoded by a single gene. Alternative RNA splicing has been reported at three sites, ED (extra type III domain)-A, ED-B, and the variable or V region. Articular cartilage fibronectin monomers are rarely (ED-A)+, but approximately 25% are (ED-B)+. RNA gel electrophoresis and Northern blot analysis identified two (ED-B)+ and two (ED-B)− fibronectin transcripts in cartilage, each pair differing by ~750 bases. This difference results from a previously unreported RNA splicing pattern that eliminates not only the V region but also nucleotides encoding protein segments III-15 and I-10. This new splice variant, which we designate (V+C)−, represents the majority of fibronectin transcripts in equine, canine, and rabbit articular cartilage but is absent in the liver. Reverse transcriptase-polymerase chain reaction analyses of 11 additional equine tissues failed to detect the (V+C)− splice variant, except for very low levels in lymph node, bone, aorta, and skin. Furthermore, chondrocytes grown in monolayer culture maintain high levels of fibronectin expression but stop expressing (V+C)− transcripts over time. The tissue-specific expression pattern of this novel fibronectin isoform suggests that it may have an important function in the matrix organization of cartilage. INTRODUCTIONFibronectin (FN) 1The abbreviations used are: FNfibronectinEDextra type III domainPCRpolymerase chain reactionRTreverse transcriptasekbkilobase(s). is an extracellular matrix glycoprotein present in body tissues and fluids. Functionally, it is important in such diverse activities as cell adhesion, cell migration, cellular differentiation, blood clotting, opsonization, wound healing, and neoplastic transformation (Hynes, 10Hynes R.O. Fibronectins. Springer-Verlag, New York Inc., New York1990Crossref Google Scholar). Fibronectin protein structure consists predominantly of three types of homologous repeating units (designated I, II, and III). It is encoded by a single gene, but significant protein heterogeneity results from alternative splicing of the pre-mRNA at three sites, termed extra type III domain A (ED-A), extra type III domain B (ED-B), and the variable (V) region (Schwarzbauer, 22Schwarzbauer J.E. Bioessays. 1991; 13: 527-533Crossref PubMed Scopus (119) Google Scholar). The V region is sometimes also referred to as the connecting segment between the 14th and 15th type III homologous repeats (IIICS). Exons encoding ED-A and ED-B are spliced in or out in their entirety. In the V region of rat FN transcripts, however, a single 5′-splice donor site combines with one of three different 3′-splice acceptor sites (exon subdivision). In the human, an additional internal 5′-splice donor site is present and results in two more V region splice variants (Vibe-Pedersen et al., 26Vibe-Pedersen K. Kornblihtt A.R. Baralle F.E. EMBO J. 1984; 3: 2511-2516Crossref PubMed Scopus (70) Google Scholar; Kornblihtt et al., 12Kornblihtt A.R. Umezawa K. Vibe-Pedersen K. Baralle F.E. EMBO J. 1985; 4: 1755-1759Crossref PubMed Scopus (468) Google Scholar; Odermatt et al., 18Odermatt E. Tamkun J.W. Hynes R.O. Proc. Natl. Acad. Sci. U. S. A. 1985; 82: 6571-6575Crossref PubMed Scopus (57) Google Scholar; Schwarzbauer et al., 24Schwarzbauer J.E. Patel R.S. Fonda D. Hynes R.O. EMBO J. 1987; 6: 2573-2580Crossref PubMed Scopus (236) Google Scholar).Fibronectin is an important matrix constituent in cartilage, and its content is markedly elevated in articular cartilage lesions within osteoarthritic joints (Wurster and Lust, 28Wurster N.B. Lust G. Biochem. Biophys. Res. Commun. 1982; 109: 1094-1101Crossref PubMed Scopus (56) Google Scholar; Burton-Wurster et al., 5Burton-Wurster N. Butler M. Harter S.J. Colombo C. Quintavalla J. Swartzendurber D. Arsenis C. Lust G. J. Rheumatol. 1986; 13: 175-182PubMed Google Scholar). Although the precise functional role of FN in normal and diseased cartilage is unknown, several unique structural features have been described. Relatively high levels of the (ED-B)+ isoform have been found in both canine and human cartilage FN (Burton-Wurster et al., 7Burton-Wurster N. Lust G. Wert R. Biochem. Biophys. Res. Commun. 1989; 165: 782-787Crossref PubMed Scopus (26) Google Scholar; Zhang et al., 29Zhang D. Burton-Wurster N. Lust G. J. Biol. Chem. 1995; 270 (a): 1817-1822Abstract Full Text Full Text PDF PubMed Scopus (29) Google Scholar; Zhang et al., 30Zhang D. Burton-Wurster N. Lust G. Matrix Biol. 1995; 14 (b): 623-633Crossref PubMed Scopus (13) Google Scholar; Rencic et al., 20Rencic A. Gehris A.L. Lewis S.D. Hume E.L. Bennett V.D. Osteoarth. Cart. 1995; 3: 187-196Abstract Full Text PDF PubMed Scopus (13) Google Scholar). A small subset of cartilage FN appears to be post-translationally modified with the addition of a chondroitin or dermatan sulfate glycosaminoglycan (Burton-Wurster and Lust, 4Burton-Wurster N. Lust G. Arch. Biochem. Biophys. 1993; 306: 309-320Crossref PubMed Scopus (9) Google Scholar). We have also observed that canine cartilage FN has a subunit with an apparent molecular mass ~15 kDa less than the smallest subunit of plasma FN. This subunit fails to react with two monoclonal antibodies that recognize epitopes in the III-15 segment, although at least some of these smaller subunits were still found within FN dimers (Burton-Wurster and Lust, 3Burton-Wurster N. Lust G. Arch. Biochem. Biophys. 1989; 269: 32-45Crossref PubMed Scopus (28) Google Scholar). These protein data are consistent with those of a subunit that retains the two sulfhydryl groups in the carboxyl terminus necessary for dimerization but has an internal deletion of the III-15 segment. In this study, we have examined the alternative splicing patterns of FN mRNA in articular cartilage. The results demonstrate a previously unreported splice variant that extends beyond any of the known 3′-acceptor sites in the V region and deletes nucleotides that would normally encode the 15th type III homology repeat (III-15) and the 10th type I homology repeat (I-10). This new splicing pattern is present in a majority of FN transcripts within articular cartilage and accounts for the small subunit of FN protein previously described.DISCUSSIONIn this report, we demonstrate a new FN splicing pattern in articular cartilage that extends beyond the normal V region. This new FN splice variant is not present in the liver and is lost over time when chondrocytes are removed from their extracellular matrix and placed in monolayer cultures. We have termed this splice variant (V+C)−. “C” denotes the cartilage-sensitive region that includes 411 nucleotides that would normally be translated into the III-15 and I-10 segments in FN protein. The absence of nucleotides encoding III-15 in the (V+C)− splice variant readily explains our previous observation that two monoclonal antibodies specific for epitopes within this segment fail to recognize the small cartilage FN protein subunits in Western blots (Burton-Wurster and Lust, 3Burton-Wurster N. Lust G. Arch. Biochem. Biophys. 1989; 269: 32-45Crossref PubMed Scopus (28) Google Scholar).Chondrocytes cultured in monolayer for up to 46 days demonstrate a progressive decrease in steady-state levels of (V+C)− FN broadly parallel to the loss of type II procollagen expression. Since an RT-PCR assay was used to follow the changes in FN splicing, however, these data do not determine exact quantitative relationships. Alternative splicing of ED-A has previously been associated with chondrocyte de-differentiation. (ED-A)+ FN is not normally expressed in cartilage but appears when chondrocytes are cultured and is further increased in passaged monolayer cells (Burton-Wurster et al., 6Burton-Wurster N. Leipold H.R. Lust G. Biochem. Biophys. Res. Commun. 1988; 154: 1088-1093Crossref PubMed Scopus (20) Google Scholar; Burton-Wurster and Lust, 3Burton-Wurster N. Lust G. Arch. Biochem. Biophys. 1989; 269: 32-45Crossref PubMed Scopus (28) Google Scholar; Bennett et al., 2Bennett V.D. Pallante K.M. Adams S.L. J. Biol. Chem. 1991; 266: 5918-5924Abstract Full Text PDF PubMed Google Scholar). The expression of (ED-A)+ FN can be modulated by the addition of dibutyryl cAMP (Leipold et al., 13Leipold H.R. Burton-Wurster N. Steinmeyer J. Vernier-Singer M.S. Lust G. J. Orthop. Res. 1992; 10: 33-48Crossref PubMed Scopus (7) Google Scholar) or transforming growth factor β1 (Zhang et al., 29Zhang D. Burton-Wurster N. Lust G. J. Biol. Chem. 1995; 270 (a): 1817-1822Abstract Full Text Full Text PDF PubMed Scopus (29) Google Scholar). In contrast, (ED-B)+ FN mRNA, which is expressed at high levels by chondrocytes within articular cartilage (15-35%), remains relatively high in primary chondrocyte cultures (18%), is insensitive to the addition of transforming growth factor β1, but is decreased by the addition of dibutyryl cAMP to the culture medium (Zhang et al., 29Zhang D. Burton-Wurster N. Lust G. J. Biol. Chem. 1995; 270 (a): 1817-1822Abstract Full Text Full Text PDF PubMed Scopus (29) Google Scholar). Loss of the cartilage-specific (V+C)− splicing pattern of FN along with the appearance of the (ED-A)+ isoform may prove to be an early and even more sensitive marker of chondrocyte de-differentiation in culture than is the loss of type II procollagen and aggrecan core protein expression.Since the liver is the primary source of plasma FN, the two splice variants generated by RT/PCR from both equine and canine liver RNA are consistent with a distribution in which approximately half of the protein subunits lack the V region and half include all or a part of the V region. This is similar to what has been reported for mouse, human, rat, and cow but unlike that for the chicken in which no FN transcripts have the V region totally excluded (Schwarzbauer et al., 23Schwarzbauer J.E. Paul J.I. Hynes R.O. Proc. Natl. Acad. Sci. U. S. A. 1985; 82: 1424-1428Crossref PubMed Scopus (57) Google Scholar; Kornblihtt et al., 12Kornblihtt A.R. Umezawa K. Vibe-Pedersen K. Baralle F.E. EMBO J. 1985; 4: 1755-1759Crossref PubMed Scopus (468) Google Scholar; Norton and Hynes, 17Norton P.A. Hynes R.O. Mol. Cell. Biol. 1987; 7: 4297-4307Crossref PubMed Scopus (136) Google Scholar; Schwarzbauer, 22Schwarzbauer J.E. Bioessays. 1991; 13: 527-533Crossref PubMed Scopus (119) Google Scholar). For human and rat FN, the V region and the first half of the III-15 segment are encoded by one exon (Tamkun et al., 25Tamkun J.W. Schwarzbauer J.E. Hynes R.O. Proc. Natl. Acad. Sci. U. S. A. 1984; 81: 5140-5144Crossref PubMed Scopus (113) Google Scholar; Vibe-Pedersen et al., 27Vibe-Pedersen K. Magnusson S. Baralle F.E. FEBS Lett. 1986; 207: 287-291Crossref PubMed Scopus (26) Google Scholar). There is, however, an internal acceptor site immediately preceding the bases encoding III-15 that permits the entire V region to be spliced out. This region is conserved in the dog and horse, as is the alternative splice acceptor site that results in a deletion of the first 25 amino acids of the V region. In humans but not in the rat, an alternative splice donor site (GAG, beginning at base 881, Fig. 4A) permits deletion of the final 31 amino acids in the V region and accounts for the total of five different FN splice variants in the V region of humans versus only three in the rat. The comparable sequence in the dog and horse is GAG, which is identical to that in the rat. Loss of the invariant GT dinucleotide suggests that the dog and horse, like the rat, will have only three splice variants within the V region and not five.In addition to the smaller and cartilage-specific (V+C)− isoform, we also detected by Northern blot hybridization and RT-PCR, FN transcripts in cartilage that have a size consistent with V region splicing patterns comparable to that observed in the liver. Burton-Wurster and Lust (3Burton-Wurster N. Lust G. Arch. Biochem. Biophys. 1989; 269: 32-45Crossref PubMed Scopus (28) Google Scholar) previously estimated that cartilage FN was 80% V+. This was based on the generation of a high percentage of a 30-kDa heparin binding fragment after thermolysin digestion, reflecting the presumed insertion of the thermolysin-sensitive V region between the type III-14 and III-15 segments (Pande et al., 19Pande H. Calaycay J. Lee T.D. Legesse K. Shively J.E. Siri A. Borsi L. Zardi L. Eur. J. Biochem. 1987; 162: 403-411Crossref PubMed Scopus (18) Google Scholar). The accuracy of this assay, however, is invalidated by the deletion of the III-15 domain in the (V+C)− isoform. Therefore, based on the transcriptional results reported here, the earlier quantitative estimate of V+ appears to be much too high. Rencic et al. (20Rencic A. Gehris A.L. Lewis S.D. Hume E.L. Bennett V.D. Osteoarth. Cart. 1995; 3: 187-196Abstract Full Text PDF PubMed Scopus (13) Google Scholar) reported that FN splicing in seven human articular cartilage samples exhibited a pattern in which the V region was deleted. They would not, however, have been able to identify the (V+C)− splice variant since the antisense primer they chose for PCR amplification was within the I-10 region.From the Northern analysis data in Fig. 1, it is clear that the cartilage-specific (V+C)− splice variant may include or exclude the ED-B segment. Direct quantitation of 32P-labeled decay events on the hybridization membrane by phosphoimager analysis (Fuji BioImaging, Stamford, CT) suggests the following approximate distribution of FN transcripts in adult equine articular cartilage: 63% ((B−,A−,(V+C)−)), 21% (B+,A−,(V+C)−), 11% (B−,A−,V+/−,C+), and 5% (B+,A−,V+/−,C+). In total, the 26:74 ratio of B+:B− transcripts is entirely consistent with published observations (Zhang et al., 29Zhang D. Burton-Wurster N. Lust G. J. Biol. Chem. 1995; 270 (a): 1817-1822Abstract Full Text Full Text PDF PubMed Scopus (29) Google Scholar, Rencic et al., 20Rencic A. Gehris A.L. Lewis S.D. Hume E.L. Bennett V.D. Osteoarth. Cart. 1995; 3: 187-196Abstract Full Text PDF PubMed Scopus (13) Google Scholar). It is also interesting to note that the percentage of (ED-B)+ transcripts is 25% in (V+C)− splice variants, which is roughly comparable to the 31% in the V+/−,C+ splice variants. Based on the observed patterns of alternative RNA splicing, the predicted major protein isoforms of FN expressed in adult equine articular cartilage are summarized in Fig. 8. PCR data with primer pair 6 also support, however, the presence of other minor V region splice variants in cartilage (Figs. 2, 3, and 7). These minor variants were not independently resolved by our Northern blot analyses. The possibility of subdivisions within the C region (nucleotides encoding III-15 and I-10) must also be considered and is not resolved by these data.Functions for some of the splice variants in the V region have been investigated and include the identification of sites that are important for cell adhesion and FN dimer secretion and the ability to affect covalent cross-linking in fibrin clots (Schwarzbauer, 22Schwarzbauer J.E. Bioessays. 1991; 13: 527-533Crossref PubMed Scopus (119) Google Scholar). Functions for the ED-B and ED-A regions remain speculative but may be related to the assembly of FN dimers into pre-existing matrices. Consistent with that idea, Zhang et al. (30Zhang D. Burton-Wurster N. Lust G. Matrix Biol. 1995; 14 (b): 623-633Crossref PubMed Scopus (13) Google Scholar) have shown that newly synthesized (ED-B)+ FN is preferentially retained in the cartilage matrix compared with that of (ED-B)− FN.The tissue-specific pattern of (V+C)− expression and its loss by chondrocytes in monolayer culture suggest that this FN isoform may play an important role in articular cartilage matrix organization. It is not yet known if the (V+C)− splice variant is also a predominant isoform in other cartilaginous tissues such as meniscal, nasal, costal, and tracheal cartilage. Tracheal cartilage in particular will be of interest since Zhang et al. (29Zhang D. Burton-Wurster N. Lust G. J. Biol. Chem. 1995; 270 (a): 1817-1822Abstract Full Text Full Text PDF PubMed Scopus (29) Google Scholar) found that it is the only cartilaginous tissue that does not express the (ED-B)+ isoform of FN. At present, we have no idea what properties the loss of the III-15 and I-10 segments may confer on the mature FN protein. The III-15 domain contains a sulfhydryl group that may be involved with intermolecular disulfide bonding, although there is some evidence to the contrary (Morla et al., 15Morla A. Zhang Z. Ruoslahti E. Nature. 1994; 367: 193-196Crossref PubMed Scopus (265) Google Scholar). Ichihara-Tanaka et al. (11Ichihara-Tanaka K. Titani K. Sekiguchi K. J. Cell Sci. 1995; 108: 907-915Crossref PubMed Google Scholar) recently reported that III-15 and the I-10 through I-12 segments are actively involved in matrix assembly and that deletion of only one of the three type I segments will markedly impair matrix assembly activity. A disulfide cross-linked “super-fibronectin” with enhanced adhesive properties (Morla et al. 15Morla A. Zhang Z. Ruoslahti E. Nature. 1994; 367: 193-196Crossref PubMed Scopus (265) Google Scholar) may be close to the natural matrix form of FN but may be inappropriate for cartilage. In addition, the juxtaposition of the III-14 and I-11 segments in the (V+C)− isoform of FN, which replaces the I-10 and I-11 junction, predicts amino acid substitutions of an acidic glutamate for a basic lysine residue in the equine and canine sequences and a glycine residue for the basic arginine residue in humans (Fig. 4B). When combined, these changes may result in alterations of the FN tertiary structure that convey additional new properties to this isoform. FN fragments but not intact FN have been reported to induce the synthesis of proteolytic enzymes in cartilage explants (Homandberg et al., 9Homandberg G.A. Meyers R. Xie D. J. Biol. Chem. 1992; 267: 3597-3604Abstract Full Text PDF PubMed Google Scholar). If the (V+C)− splice variant mimics a FN fragment in this regard, it may have an important regulatory role to play in matrix metalloproteinase activity within articular cartilage. Although these and other possibilities need to be independently investigated, the tissue-specific pattern of (V+C)− FN expression suggests that this isoform has an important function in articular cartilage. INTRODUCTIONFibronectin (FN) 1The abbreviations used are: FNfibronectinEDextra type III domainPCRpolymerase chain reactionRTreverse transcriptasekbkilobase(s). is an extracellular matrix glycoprotein present in body tissues and fluids. Functionally, it is important in such diverse activities as cell adhesion, cell migration, cellular differentiation, blood clotting, opsonization, wound healing, and neoplastic transformation (Hynes, 10Hynes R.O. Fibronectins. Springer-Verlag, New York Inc., New York1990Crossref Google Scholar). Fibronectin protein structure consists predominantly of three types of homologous repeating units (designated I, II, and III). It is encoded by a single gene, but significant protein heterogeneity results from alternative splicing of the pre-mRNA at three sites, termed extra type III domain A (ED-A), extra type III domain B (ED-B), and the variable (V) region (Schwarzbauer, 22Schwarzbauer J.E. Bioessays. 1991; 13: 527-533Crossref PubMed Scopus (119) Google Scholar). The V region is sometimes also referred to as the connecting segment between the 14th and 15th type III homologous repeats (IIICS). Exons encoding ED-A and ED-B are spliced in or out in their entirety. In the V region of rat FN transcripts, however, a single 5′-splice donor site combines with one of three different 3′-splice acceptor sites (exon subdivision). In the human, an additional internal 5′-splice donor site is present and results in two more V region splice variants (Vibe-Pedersen et al., 26Vibe-Pedersen K. Kornblihtt A.R. Baralle F.E. EMBO J. 1984; 3: 2511-2516Crossref PubMed Scopus (70) Google Scholar; Kornblihtt et al., 12Kornblihtt A.R. Umezawa K. Vibe-Pedersen K. Baralle F.E. EMBO J. 1985; 4: 1755-1759Crossref PubMed Scopus (468) Google Scholar; Odermatt et al., 18Odermatt E. Tamkun J.W. Hynes R.O. Proc. Natl. Acad. Sci. U. S. A. 1985; 82: 6571-6575Crossref PubMed Scopus (57) Google Scholar; Schwarzbauer et al., 24Schwarzbauer J.E. Patel R.S. Fonda D. Hynes R.O. EMBO J. 1987; 6: 2573-2580Crossref PubMed Scopus (236) Google Scholar).Fibronectin is an important matrix constituent in cartilage, and its content is markedly elevated in articular cartilage lesions within osteoarthritic joints (Wurster and Lust, 28Wurster N.B. Lust G. Biochem. Biophys. Res. Commun. 1982; 109: 1094-1101Crossref PubMed Scopus (56) Google Scholar; Burton-Wurster et al., 5Burton-Wurster N. Butler M. Harter S.J. Colombo C. Quintavalla J. Swartzendurber D. Arsenis C. Lust G. J. Rheumatol. 1986; 13: 175-182PubMed Google Scholar). Although the precise functional role of FN in normal and diseased cartilage is unknown, several unique structural features have been described. Relatively high levels of the (ED-B)+ isoform have been found in both canine and human cartilage FN (Burton-Wurster et al., 7Burton-Wurster N. Lust G. Wert R. Biochem. Biophys. Res. Commun. 1989; 165: 782-787Crossref PubMed Scopus (26) Google Scholar; Zhang et al., 29Zhang D. Burton-Wurster N. Lust G. J. Biol. Chem. 1995; 270 (a): 1817-1822Abstract Full Text Full Text PDF PubMed Scopus (29) Google Scholar; Zhang et al., 30Zhang D. Burton-Wurster N. Lust G. Matrix Biol. 1995; 14 (b): 623-633Crossref PubMed Scopus (13) Google Scholar; Rencic et al., 20Rencic A. Gehris A.L. Lewis S.D. Hume E.L. Bennett V.D. Osteoarth. Cart. 1995; 3: 187-196Abstract Full Text PDF PubMed Scopus (13) Google Scholar). A small subset of cartilage FN appears to be post-translationally modified with the addition of a chondroitin or dermatan sulfate glycosaminoglycan (Burton-Wurster and Lust, 4Burton-Wurster N. Lust G. Arch. Biochem. Biophys. 1993; 306: 309-320Crossref PubMed Scopus (9) Google Scholar). We have also observed that canine cartilage FN has a subunit with an apparent molecular mass ~15 kDa less than the smallest subunit of plasma FN. This subunit fails to react with two monoclonal antibodies that recognize epitopes in the III-15 segment, although at least some of these smaller subunits were still found within FN dimers (Burton-Wurster and Lust, 3Burton-Wurster N. Lust G. Arch. Biochem. Biophys. 1989; 269: 32-45Crossref PubMed Scopus (28) Google Scholar). These protein data are consistent with those of a subunit that retains the two sulfhydryl groups in the carboxyl terminus necessary for dimerization but has an internal deletion of the III-15 segment. In this study, we have examined the alternative splicing patterns of FN mRNA in articular cartilage. The results demonstrate a previously unreported splice variant that extends beyond any of the known 3′-acceptor sites in the V region and deletes nucleotides that would normally encode the 15th type III homology repeat (III-15) and the 10th type I homology repeat (I-10). This new splicing pattern is present in a majority of FN transcripts within articular cartilage and accounts for the small subunit of FN protein previously described." @default.
• W2032961490 created "2016-06-24" @default.
• W2032961490 creator A5036783419 @default.
• W2032961490 creator A5047457069 @default.
• W2032961490 creator A5072876010 @default.
• W2032961490 creator A5083688304 @default.
• W2032961490 date "1996-08-01" @default.
• W2032961490 modified "2023-09-29" @default.
• W2032961490 title "Fibronectin mRNA Splice Variant in Articular Cartilage Lacks Bases Encoding the V, III-15, and I-10 Protein Segments" @default.
• W2032961490 cites W107731324 @default.
• W2032961490 cites W1552444104 @default.
• W2032961490 cites W1558749218 @default.
• W2032961490 cites W1605153099 @default.
• W2032961490 cites W1609575719 @default.
• W2032961490 cites W1964131020 @default.
• W2032961490 cites W1969035670 @default.
• W2032961490 cites W1983646864 @default.
• W2032961490 cites W1988493675 @default.
• W2032961490 cites W1997110396 @default.
• W2032961490 cites W2000961393 @default.
• W2032961490 cites W2013446961 @default.
• W2032961490 cites W2015950143 @default.
• W2032961490 cites W2020645507 @default.
• W2032961490 cites W2027553466 @default.
• W2032961490 cites W2033415732 @default.
• W2032961490 cites W2039059443 @default.
• W2032961490 cites W2044008951 @default.
• W2032961490 cites W2054031175 @default.
• W2032961490 cites W2062327892 @default.
• W2032961490 cites W2063338234 @default.
• W2032961490 cites W2072454059 @default.
• W2032961490 cites W2076754978 @default.
• W2032961490 cites W2122559302 @default.
• W2032961490 cites W4294216491 @default.
• W2032961490 doi "https://doi.org/10.1074/jbc.271.31.18954" @default.
• W2032961490 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/8702559" @default.
• W2032961490 hasPublicationYear "1996" @default.
• W2032961490 type Work @default.
• W2032961490 sameAs 2032961490 @default.
• W2032961490 citedByCount "75" @default.
• W2032961490 countsByYear W20329614902012 @default.
• W2032961490 countsByYear W20329614902013 @default.
• W2032961490 countsByYear W20329614902014 @default.
• W2032961490 countsByYear W20329614902015 @default.
• W2032961490 countsByYear W20329614902016 @default.
• W2032961490 countsByYear W20329614902018 @default.
• W2032961490 countsByYear W20329614902022 @default.
• W2032961490 countsByYear W20329614902023 @default.
• W2032961490 crossrefType "journal-article" @default.
• W2032961490 hasAuthorship W2032961490A5036783419 @default.
• W2032961490 hasAuthorship W2032961490A5047457069 @default.
• W2032961490 hasAuthorship W2032961490A5072876010 @default.
• W2032961490 hasAuthorship W2032961490A5083688304 @default.
• W2032961490 hasConcept C104317684 @default.
• W2032961490 hasConcept C105580179 @default.
• W2032961490 hasConcept C105702510 @default.
• W2032961490 hasConcept C142724271 @default.
• W2032961490 hasConcept C153911025 @default.
• W2032961490 hasConcept C185592680 @default.
• W2032961490 hasConcept C189165786 @default.
• W2032961490 hasConcept C204787440 @default.
• W2032961490 hasConcept C2776164576 @default.
• W2032961490 hasConcept C2780550940 @default.
• W2032961490 hasConcept C2780989783 @default.
• W2032961490 hasConcept C3020332539 @default.
• W2032961490 hasConcept C54355233 @default.
• W2032961490 hasConcept C54458228 @default.
• W2032961490 hasConcept C67705224 @default.
• W2032961490 hasConcept C70721500 @default.
• W2032961490 hasConcept C71924100 @default.
• W2032961490 hasConcept C86492073 @default.
• W2032961490 hasConcept C86803240 @default.
• W2032961490 hasConcept C95444343 @default.
• W2032961490 hasConceptScore W2032961490C104317684 @default.
• W2032961490 hasConceptScore W2032961490C105580179 @default.
• W2032961490 hasConceptScore W2032961490C105702510 @default.
• W2032961490 hasConceptScore W2032961490C142724271 @default.
• W2032961490 hasConceptScore W2032961490C153911025 @default.
• W2032961490 hasConceptScore W2032961490C185592680 @default.
• W2032961490 hasConceptScore W2032961490C189165786 @default.
• W2032961490 hasConceptScore W2032961490C204787440 @default.
• W2032961490 hasConceptScore W2032961490C2776164576 @default.
• W2032961490 hasConceptScore W2032961490C2780550940 @default.
• W2032961490 hasConceptScore W2032961490C2780989783 @default.
• W2032961490 hasConceptScore W2032961490C3020332539 @default.
• W2032961490 hasConceptScore W2032961490C54355233 @default.
• W2032961490 hasConceptScore W2032961490C54458228 @default.
• W2032961490 hasConceptScore W2032961490C67705224 @default.
• W2032961490 hasConceptScore W2032961490C70721500 @default.
• W2032961490 hasConceptScore W2032961490C71924100 @default.
• W2032961490 hasConceptScore W2032961490C86492073 @default.
• W2032961490 hasConceptScore W2032961490C86803240 @default.
• W2032961490 hasConceptScore W2032961490C95444343 @default.
• W2032961490 hasIssue "31" @default.
• W2032961490 hasLocation W20329614901 @default.
• W2032961490 hasOpenAccess W2032961490 @default.
• W2032961490 hasPrimaryLocation W20329614901 @default.
• W2032961490 hasRelatedWork W1864764602 @default.

• next