{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,17]],"date-time":"2026-08-17T14:49:03Z","timestamp":1786978143381,"version":"build-2736575974"},"reference-count":69,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2003,3,27]],"date-time":"2003-03-27T00:00:00Z","timestamp":1048723200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Microscopy Res &amp; Technique"],"published-print":{"date-parts":[[2003,5]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\n                    Testicular spermatozoa undergo morphological and biochemical alterations, collectively termed epididymal maturation, in the intraluminal environment of epididymis. As a result of these modifications, the spermatozoon becomes a motile and functionally competent cell capable of undergoing capacitation and binding to the zona pellucida, the extracellular coat that surrounds the mammalian oocyte. Although details of all the changes are not fully known, several studies provide evidence suggesting that sperm plasma membrane undergoes extensive biochemical changes, including organization and modification of surface glycoproteins as spermatozoa transit from the proximal to the distal epididymis. In this article, I have attempted to summarize results with two sets of glycoprotein (glycan)\u2010modifying enzymes, namely, glycohydrolases (hydrolytic enzymes) and glycosyltransferases (synthetic enzymes) present in the epididymal luminal fluid (LF). The in vitro experimental approaches described in this report demonstrate that: 1) a PNA\u2010positive glycoprotein(s) (containing O\u2010linked glycan) of 135\u2013150 kDa subunit molecular mass which is present on the surface of caput (but not the cauda) spermatozoa can be degalactosylated by the enzymatic digestion with LF \u03b2\u2010D\u2010galactosidase; and 2) an N\u2010linked glycan chain(s) which is present on a sperm surface glycoprotein (apparent subunit molecular mass of 86 kDa) can be fucosylated in vitro when distal caput sperm (or sperm plasma membrane\u2010rich fractions) are incubated in the presence of a nucleotide sugar (GDP[\n                    <jats:sup>14<\/jats:sup>\n                    C]fucose). Combined, these results strongly suggest a role for the glycan\u2010modifying enzymes in degalactosylation and fucosylation of sperm surface glycoproteins during epididymal transit. Microsc. Res. Tech. 61:18\u201327, 2003. \u00a9 2003 Wiley\u2010Liss, Inc.\n                  <\/jats:p>","DOI":"10.1002\/jemt.10313","type":"journal-article","created":{"date-parts":[[2003,3,28]],"date-time":"2003-03-28T07:54:08Z","timestamp":1048838048000},"page":"18-27","source":"Crossref","is-referenced-by-count":35,"title":["Glycan modifying enzymes in luminal fluid of rat epididymis: Are they involved in altering sperm surface glycoproteins during maturation?"],"prefix":"10.1002","volume":"61","author":[{"given":"Daulat 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