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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
|
| pubmed:dateCreated |
1996-3-5
|
| pubmed:databankReference | |
| pubmed:abstractText |
In the preceding study (Okamura et al., 1992; Biol Reprod 47:1040-1052) we suggested that a 135-kDa protein secreted by porcine epididymis is involved in the sperm maturation. In this work, we have isolated the cDNA clone coding the 135-kDa protein in an effort to investigate its structure and function. The 135-kDa protein was purified from porcine cauda epididymal fluid. Three oligonucleotide probes were synthesized according to the amino acid sequences of N-termini of the native protein and trypsin-digested peptides. A cDNA clone hybridizing with these three probes was isolated from the cDNA library derived from the porcine proximal corpus epididymis. It encodes a novel protein with 1,006 amino acid residues in an open reading frame. Its overall amino acid sequence was significantly homologous (25.7%) to the alpha-mannosidase precursor of Dictiostelium discoideum (P34098). The 135-kDa protein could digest both p-nitro-phenyl-alpha-D-mannoside and high mannose oligo saccharide (Man8-GlcNAc2), strongly suggesting that it is an alpha-mannosidase homologue. The expression of this protein was specific to porcine and was localized to the very narrow parts of epididymis: the border of the caput and corpus epididymis. This protein may serve as a good marker for the functional differentiation in porcine epididymis. A possible role of this protein in the species-specific sperm-egg interaction is discussed.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Oct
|
| pubmed:issn |
1040-452X
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
42
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
141-8
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:8562059-Amino Acid Sequence,
pubmed-meshheading:8562059-Animals,
pubmed-meshheading:8562059-Base Sequence,
pubmed-meshheading:8562059-Carbohydrate Sequence,
pubmed-meshheading:8562059-Cell Membrane,
pubmed-meshheading:8562059-Cloning, Molecular,
pubmed-meshheading:8562059-DNA, Complementary,
pubmed-meshheading:8562059-Dictyostelium,
pubmed-meshheading:8562059-Epididymis,
pubmed-meshheading:8562059-Female,
pubmed-meshheading:8562059-Male,
pubmed-meshheading:8562059-Mannosidases,
pubmed-meshheading:8562059-Molecular Sequence Data,
pubmed-meshheading:8562059-Oligosaccharides,
pubmed-meshheading:8562059-Sequence Homology, Amino Acid,
pubmed-meshheading:8562059-Sperm Maturation,
pubmed-meshheading:8562059-Sperm-Ovum Interactions,
pubmed-meshheading:8562059-Spermatozoa,
pubmed-meshheading:8562059-Substrate Specificity,
pubmed-meshheading:8562059-Swine,
pubmed-meshheading:8562059-Tissue Distribution,
pubmed-meshheading:8562059-alpha-Mannosidase
|
| pubmed:year |
1995
|
| pubmed:articleTitle |
Cloning of complementary DNA encoding a 135-kilodalton protein secreted from porcine corpus epididymis and its identification as an epididymis-specific alpha-mannosidase.
|
| pubmed:affiliation |
Institute of Basic Medical Sciences, University of Tsukuba, Ibaraki, Japan.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|