Gene expression in the dog epididymis: a model for human epididymal function

Ellerbrock, K.; Pera, I.; Hartung, Stefan; Ivell, Richard

doi:10.1111/j.1365-2605.1994.tb01262.x

Cited by 39 publications

(27 citation statements)

References 34 publications

(29 reference statements)

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“…Previous studies have shown the existence of HE4 homologues in rabbit (BE-20, U26725) (Xu et al, 1996) and dog (CE4, S77395) (Ellerbrock et al, 1994). By searching the public EST databases we were able to identify further homologues from pig (represented by BE234395), mouse (AF334269) and rat (represented by AI411527).…”

mentioning

confidence: 94%

The putative ovarian tumour marker gene HE4 (WFDC2), is expressed in normal tissues and undergoes complex alternative splicing to yield multiple protein isoforms

2002

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The whey acidic protein (WAP) domain is a conserved motif, containing eight cysteines found in a characteristic 4-disulphide core arrangement, that is present in a number of otherwise unrelated proteins. WAP motifs are present in SLPI and ela®n, two antiproteinases located on chromosome 20q12-13, in a locus rich in poorly characterized WAP domain proteins. One of these proteins, which contains two WAP domains, is HE4 (also known as WFDC2), originally described as an epididymis speci®c protein but more recently suggested to be a putative serum tumour marker for ovarian cancer. We have shown that HE4 is expressed in a number of normal human tissues outside of the male reproductive system, including regions of the respiratory tract and nasopharynx, as well as in a subset of lung tumour cell lines. Comparison of multiple HE4 cDNAs and RT ± PCR products with genomic sequence allowed the elucidation of the genomic organization. These studies revealed that HE4 can undergo a complex series of alternative splicing events that can potentially yield ®ve distinct WAP domain containing protein isoforms. These results cast doubt on the potential role of HE4 as a serum tumour marker speci®c for ovarian cancer and open the door to understanding the function of multiple WAP domain containing protein isoforms arising from a single gene.

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mentioning

confidence: 94%

The putative ovarian tumour marker gene HE4 (WFDC2), is expressed in normal tissues and undergoes complex alternative splicing to yield multiple protein isoforms

2002

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“…Proteins with an identical peptide backbone have been isolated from various primates (Perry et al, 1995;Fröhlich and Young, 1996), and represent approximately 20% of the luminal protein content of cauda epididymidal fluid in chimpanzees (Fröhlich and Young, 1996). Closely related products have been identified in non-primate species (Ellerbrock et al, 1994;Syntin et al, 1996). However, the HE1 peptide sequence seems evolutionarily to be much older; a similar protein (esr16; accession no.…”

Section: Putative Cholesterol Carriersmentioning

confidence: 99%

“…Closely related proteins have been cloned from epididymal tissue of other species (Ellerbrock et al, 1994;Xu et al, 1996). The positions of half-cysteines suggested that they are twodomain members of the 'four-disulfide core'-or 'whey acidic' protein (WAP)-domain proteins, to which the human seminal plasma proteinase inhibitor, HUSI-I/SLPI (Seemüller et al, 1986;Jin et al, 1997), and a decapacitation factor of guinea-pig spermatozoa, caltrin II, belong (Coronel and Lardy, 1992).…”

Section: Putative Secretory Proteinase Inhibitorsmentioning

confidence: 99%

Molecular characterization of epididymal proteins

Kirchhoff¹

1998

Reviews of Reproduction

156

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“…Its secretion varies with different phases of lactation (44), and it possibly plays a role in hair and nail growth (45). Although the physiological functions of epididymal proteins such as HE4, CE4, and BE20 (30,46,47) in the male genital tract are not clear, they may act as decapitation factors that bind to sperm that are released in the female reproductive tract (48).…”

Section: Discussionmentioning

confidence: 99%

Identification of a Novel Family of Proteins in Snake Venoms

Torres

Wong

Desai

et al. 2003

Journal of Biological Chemistry

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The three-dimensional structure of nawaprin has been determined by nuclear magnetic resonance spectroscopy. This 51-amino acid residue peptide was isolated from the venom of the spitting cobra, Naja nigricollis, and is the first member of a new family of snake venom proteins referred to as waprins. Nawaprin is relatively flat and disc-like in shape, characterized by a spiral backbone configuration that forms outer and inner circular segments. The two circular segments are held together by four disulfide bonds, three of which are clustered at the base of the molecule. The inner segment contains a short antiparallel ␤-sheet, whereas the outer segment is devoid of secondary structures except for a small turn or 3 10 helix. The structure of nawaprin is very similar to elafin, a human leukocyte elastase-specific inhibitor. Although substantial parts of the nawaprin molecule are well defined, the tips of the outer and inner circular segments, which are hypothesized to be critical for binding interactions, are apparently disordered, similar to that found in elafin. The amino acid residues in these important regions in nawaprin are different from those in elafin, suggesting that nawaprin is not an elastase-specific inhibitor and therefore has a different function in the snake venom.Snake venoms are rich sources of pharmacologically active polypeptides and proteins. Some of these proteins exhibit enzymatic activities. These enzymes include phospholipase A 2 , proteinase, nucleotidase, phosphodiesterase, and L-amino acid oxidase. In addition to their catalytic properties that may contribute to the digestive action of the venom, these enzymes also induce various pharmacological effects including neurotoxic, myotoxic, cardiotoxic, hemorrhagic, hemolytic, procoagulant, and anticoagulant effects (1, 2). Several other snake venom proteins and polypeptides do not exhibit these and other enzymatic activities and thus are described as "nonenzymatic proteins." These proteins include neurotoxins, cardiotoxins, myotoxins, ion channel inhibitors, and anticoagulant proteins (3, 4). Thus, snake venom proteins, whether they are enzymatic or nonenzymatic, have evolved as a complex mixture of proteins that target several tissues, organs, and physiological systems and interfere in their normal functions. Therefore snake venoms, when injected into a prey or victim, result in the simultaneous assault on various tissues, leading to multiple organ or system failure and often death.A large number of protein toxins have been purified and characterized from snake venoms. These studies have shown that each venom contains over a hundred protein toxins. These toxins, however, belong to a very small number of superfamilies of proteins. For example, a single snake venom can contain as many as 15 isoforms of phospholipase A 2 (5-7). As one would expect, they share remarkable similarities in their primary, secondary, and tertiary structures. However, at times they differ from each other in their biological targeting and hence their pharmacological effec...

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Gene expression in the dog epididymis: a model for human epididymal function

Cited by 39 publications

References 34 publications

The putative ovarian tumour marker gene HE4 (WFDC2), is expressed in normal tissues and undergoes complex alternative splicing to yield multiple protein isoforms

The putative ovarian tumour marker gene HE4 (WFDC2), is expressed in normal tissues and undergoes complex alternative splicing to yield multiple protein isoforms

Molecular characterization of epididymal proteins

Identification of a Novel Family of Proteins in Snake Venoms

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