Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P56851 (epididymal)
 11,273 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The effect of dietary fats on phospholipid class distribution and fatty acid composition was studied in rat fat cell plasma membrane. Three groups of male Wistar weanling rats were fed for 8 wk three diets differing in the amount and nature of the fats: 1.5% sunflower oil (low fat control; LFC), 10% sunflower oil (high fat, unsaturated; HFU), 1.5% sunflower oil + 8.5% cocoa butter (high fat, saturated; HFS). Plasma membranes were prepared from epididymal adipocytes. The amount and type of dietary fat significantly altered membrane phospholipid distribution. Phospholipid content was lowered with HFU as compared to LFC or HFS diets, but no changes were observed for cholesterol. Phosphatidylinositol (PI) and phosphatidylserine (PS) were less affected by dietary changes than were other phospholipid classes. Major changes were detected for phosphatidylcholine (PC), phosphatidylethanolamine (PE) and sphingomyelin (SM) contents. No large changes in PC and PE fatty acid compositions were observed between the LFC and HFS groups, but the HFU diet induced several changes. Correlations with plasma membrane 5'-nucleotidase activities are discussed.
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PMID:Effect of dietary fat on phospholipid class distribution and fatty acid composition in rat fat cell plasma membrane. 235 53

Gp20 is a sialylglycoprotein of the human sperm surface related to maturation and capacitation and is homologous to CD52, a glycosyl- phosphatidyl-inositol (GPI)-anchored protein highly expressed in lymphocytes, monocytes, eosinophils, and epididymal cells, described by the monoclonal antibody family CAMPATH. The CAMPATH antigen is characterized by a very short peptide (12 amino acids) and an N-linked oligosaccharide chain bound to the asparagine located in the third position and a GPI anchor bound to the C-terminal serine. The CAMPATH epitope includes three amino acids at the C-terminus and part of the GPI anchor. It has been suggested that anti-gp20 interacts with the same peptide recognized by CAMPATH antibodies but with a different epitope, since it describes the corresponding antigen in a different way. For example, it localizes the corresponding antigen in the equatorial region of the sperm head when sperm are capacitated, whereas CAMPATH antibodies bind all over the sperm surface. Our results indicate that the anti-gp20 epitope does not include the peptide backbone, the GPI anchor, or the N-glycans but consists of O-linked oligosaccharide chains bound to a unique CD52 glycoform present both in sperm and leukocytes. This is suggested by results obtained using many different approaches, such as immunoblot analysis of gp20 after removal of N- and O-glycans and after jacalin (Artocarpus integrifolia agglutinin)-affinity chromatography.
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PMID:Epitope analysis of immunoglobulins against gp20, a GPI-anchored protein of the human sperm surface homologous to leukocyte antigen CD52. 1610 32

During the epididymal maturation, spermatozoa interact with different populations of epididymosomes and sequentially acquire some epididymosome-associated proteins critical to sperm functions. Although very few proteins associated with epididymosomes have been identified, the physiological importance of these vesicles in the sperm maturation remains unclear. To document these relevant issues, lipid and protein analysis of epididymosomes from caput and cauda epididymal fluids was determined. Lipid analysis revealed a particular composition of specific phospholipids in these vesicles; the levels of phosphatidyl-ethanolamine, phosphatidyl-inositol and phosphatidyl-choline being higher in caput epididymosomes. From the 555 and 438 proteins identified in caput- and cauda-derived epididymosomes, respectively, 231 proteins were identified in both types of epididymosome. Proteins exclusively identified in caput and cauda epididymosomes are mainly enzymes and transporter molecules. The presence of several glycan-modifying enzymes is the hallmark of the caput epididymosomes proteome. Among the common proteins in both types of epididymosome, a subset of Rab and SNARE proteins implicated in vesicle trafficking and membrane fusion were identified. Together, these data suggest that epididymosome-associated proteins are involved in various molecular functions suggesting that during the epididymal transit, spermatozoa interact with different populations of epididymosomes, which could modify the male gamete in a sequential manner.
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PMID:Comparative proteome and lipid profiles of bovine epididymosomes collected in the intraluminal compartment of the caput and cauda epididymidis. 2187 28