FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2100133669> ?p ?o ?g. }

• W2100133669 endingPage "801" @default.
• W2100133669 startingPage "786" @default.
• W2100133669 abstract "During spermiogenesis, the elongating rat spermatid chromatin undergoes a gradual process of condensation which is initiated in the round spermatids at “step 7” of cytodifferentation in stage VII and extending to elongated spermatids at “step 19” of cytodifferentiation in stage VIII. The mechanism of chromatin condensation in the elongating spermatids is an elaborate process that encompasses several biochemical and biological aspects culminating in the deposition of protamine in DNA grooves. The protamination of sperm chromatin involves expression and storage of proteins involved in condensation, removal and degradation of nuclear histones and their replacement by transition proteins and protamine 1, transcriptional silencing and DNA repair, reduction of nuclear volume, repackaging of protaminated chromatin in torroids and development of a characteristic head shape and perforatorium. A study was undertaken in my laboratory to delineate the role of follicle stimulating hormone (FSH) and testosterone in the condensation of nuclear chromatin in the elongating spermatids of sexually competent rat. Towards this end, sexually competent male Holtzmann rats were treated with 20 mg/Kg/d per os (oral supplementum) of cyproterone acetate and 3 mg/Kg/d i.p (intra peritoneal) of fluphenazine decanoate to induce a functional deficiency in either testosterone or FSH. In both rat models, membrane-impermeable CMA3 fluorescent dye uptake assay for GC-rich prospective sites of DNA protamination, was indicative of insufficiency of protamine 1 in spermatozoa taken from caput epididymides of treated rats whereas a fluorescent TUNEL assay indicated the presence of nicked chromatin strands only in protamine-deficient spermatozoa derived from caput epididymides of fluphenazine-treated rats with functional deficiency of FSH. Western blotting of acid-soluble sperm basic proteins had confirmed the near absence of protamine 1 in treated rat spermatozoa in both models. Electron Microscopic evaluation too revealed fine ultrastructural changes in the nuclear membrane of cyproterone acetate as well as fluphenazine decanoate treated spermatozoa derived from caput epididymides. Electrophoretic analysis of caput sperm nuclear basic proteins substantiated the observations at cellular level and revealed a pattern of abnormal persistence of acid-soluble nuclear basic proteins in both rat models, the levels being more prominent in fluphenazine treated rats. Our studies suggest that adequate levels of both FSH and testosterone could be essential during the stages of spermatidal condensation and led us to hypothesize the existence of an endocrine-regulated molecular mechanism for histone to protamine transition and maintenance of chromatin integrity during chromatin condensation in the testis during spermiogenesis. Keywords: Spermiogenesis, chromatin condensation, histones, protamine, cyproterone acetate, fluphenazine decanoate, follicle stimulating hormone, testosterone, spermatogonia, spermatozoa, post-meiotic spermatids, Spermiation, Sertoli cells, transcriptional silencing, Polyubiquitylated histones, Sperm Chromatin Protamination, azoospermia, sperm chromatin structural assay, HUP1N, Testosterone synergism, transcription, transcriptional arrest, Histone acetyl transferases (HATs)Spermiogenesis, chromatin condensation, histones, protamine, cyproterone acetate, fluphenazine decanoate, follicle stimulating hormone, testosterone, spermatogonia, spermatozoa, post-meiotic spermatids, Spermiation, Sertoli cells, transcriptional silencing, Polyubiquitylated histones, Sperm Chromatin Protamination, azoospermia, sperm chromatin structural assay, HUP1N, Testosterone synergism, transcription, transcriptional arrest, Histone acetyl transferases (HATs)" @default.
• W2100133669 created "2016-06-24" @default.
• W2100133669 creator A5047658617 @default.
• W2100133669 creator A5058266715 @default.
• W2100133669 creator A5061882634 @default.
• W2100133669 date "2011-08-01" @default.
• W2100133669 modified "2023-09-27" @default.
• W2100133669 title "Sperm Chromatin Protamination: An Endocrine Perspective" @default.
• W2100133669 cites W119377168 @default.
• W2100133669 cites W1483955803 @default.
• W2100133669 cites W1487878375 @default.
• W2100133669 cites W1500224677 @default.
• W2100133669 cites W1503716060 @default.
• W2100133669 cites W1515084688 @default.
• W2100133669 cites W1515962766 @default.
• W2100133669 cites W1522635297 @default.
• W2100133669 cites W1523020100 @default.
• W2100133669 cites W1523268419 @default.
• W2100133669 cites W1525654309 @default.
• W2100133669 cites W1527223628 @default.
• W2100133669 cites W1559313501 @default.
• W2100133669 cites W1567517848 @default.
• W2100133669 cites W1582270874 @default.
• W2100133669 cites W1585741829 @default.
• W2100133669 cites W1607710027 @default.
• W2100133669 cites W196600856 @default.
• W2100133669 cites W1966502376 @default.
• W2100133669 cites W1969140317 @default.
• W2100133669 cites W1969561254 @default.
• W2100133669 cites W1972914977 @default.
• W2100133669 cites W1973916462 @default.
• W2100133669 cites W1977815876 @default.
• W2100133669 cites W1977847006 @default.
• W2100133669 cites W1980300512 @default.
• W2100133669 cites W1981916517 @default.
• W2100133669 cites W1983951002 @default.
• W2100133669 cites W198495166 @default.
• W2100133669 cites W1986721429 @default.
• W2100133669 cites W1987577750 @default.
• W2100133669 cites W1994736923 @default.
• W2100133669 cites W2002890692 @default.
• W2100133669 cites W2004457392 @default.
• W2100133669 cites W2004885094 @default.
• W2100133669 cites W2005047818 @default.
• W2100133669 cites W2006239074 @default.
• W2100133669 cites W2009221759 @default.
• W2100133669 cites W2013386406 @default.
• W2100133669 cites W2016973336 @default.
• W2100133669 cites W2017921735 @default.
• W2100133669 cites W2020532280 @default.
• W2100133669 cites W2021277982 @default.
• W2100133669 cites W2026553604 @default.
• W2100133669 cites W2027541222 @default.
• W2100133669 cites W2028029982 @default.
• W2100133669 cites W2029386921 @default.
• W2100133669 cites W2029601224 @default.
• W2100133669 cites W2030195891 @default.
• W2100133669 cites W2030622242 @default.
• W2100133669 cites W2032698806 @default.
• W2100133669 cites W2033350100 @default.
• W2100133669 cites W2035069455 @default.
• W2100133669 cites W2037115203 @default.
• W2100133669 cites W2041110235 @default.
• W2100133669 cites W2041452638 @default.
• W2100133669 cites W2041959173 @default.
• W2100133669 cites W2042537337 @default.
• W2100133669 cites W2043402151 @default.
• W2100133669 cites W2043622843 @default.
• W2100133669 cites W2043855098 @default.
• W2100133669 cites W2047760682 @default.
• W2100133669 cites W2047837922 @default.
• W2100133669 cites W2049378688 @default.
• W2100133669 cites W2049654874 @default.
• W2100133669 cites W2051659471 @default.
• W2100133669 cites W2052019435 @default.
• W2100133669 cites W2055883508 @default.
• W2100133669 cites W2059710665 @default.
• W2100133669 cites W2060310965 @default.
• W2100133669 cites W2060336856 @default.
• W2100133669 cites W2063637086 @default.
• W2100133669 cites W2066118199 @default.
• W2100133669 cites W2069695937 @default.
• W2100133669 cites W2070440036 @default.
• W2100133669 cites W2072177313 @default.
• W2100133669 cites W2072697652 @default.
• W2100133669 cites W2075009635 @default.
• W2100133669 cites W2077251269 @default.
• W2100133669 cites W2077875823 @default.
• W2100133669 cites W2079291593 @default.
• W2100133669 cites W2080240363 @default.
• W2100133669 cites W2081114467 @default.
• W2100133669 cites W2082636922 @default.
• W2100133669 cites W2082698283 @default.
• W2100133669 cites W2083898957 @default.
• W2100133669 cites W2084765400 @default.
• W2100133669 cites W2086877448 @default.
• W2100133669 cites W2087736942 @default.
• W2100133669 cites W2089682454 @default.

• next