The γ-trace concentration of normal human seminal plasma is thirty-six times that of normal human blood plasma

Grubb, Anders; Weiber, Håkan; Löfberg, Helge

doi:10.1080/00365518309168281

Cited by 13 publications

(14 citation statements)

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“…A probable initiator methionine, located six nucleotides downstream of a stop codon and flanked by sequences in agreement with the Kozak initiation consensus [26], is coded for by nucleotides 78-80. An open reading frame extending from the postulated initiator methionine to a stop codon, TAG, at positions 516-518, encodes the 120 amino acids of cystatin C isolated from urine [13,14] and a putative hydrophobic signal sequence of 26 amino acid residues.…”

Section: Resultsmentioning

confidence: 99%

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Molecular cloning and sequence analysis of cDNA coding for the precursor of the human cysteine proteinase inhibitor cystatin C

et al. 1987

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Recombinant cystatin C producing clones were isolated from a human placenta llgtl 1 cDNA library. The cDNA insert of one of the clones, containing 777 base pairs, encodes the complete mature cystatin C (120 amino acids) and a hydr*ophobic leader sequence of 26 amino acids, indicating an extracellular function of the inhibitor. The deduced protein sequence confirms the protein sequence of cystatin C isolated from human urine, but differs in one position from the sequence of the cystatin C fragment deposited as amyloid in hereditary cerebral hemorrhage with amyloidosis.

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Section: Resultsmentioning

confidence: 99%

“…pa~&_@r&~~ 0% hereditary cerebral hermorrhage with amyloidosis 11%13). 7%~ amino acid segaence 02 cy&&in C isolated from human urine [13,14] was recently PeppW$ed tD be hDLQdDgD2B Wi&' C-HZ2-7&'S DRCDgene products 1151.…”

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confidence: 99%

Molecular cloning and sequence analysis of cDNA coding for the precursor of the human cysteine proteinase inhibitor cystatin C

et al. 1987

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“…It has been localized immunocytochemically in some cortical neurons, LH cells of the adenohypophysis, pancreatic A and thyroid C cells, and adrenal medulla (3). It is secreted into tissue culture medium by monocytes and other cells, and the down-regulation of its secretion may play a role in inflammation (4).…”

Section: Introductionmentioning

confidence: 99%

Binding of cystatin C to C4: the importance of sense-antisense peptides in their interaction.

Ghiso

Saball

Leoni

et al. 1990

Proc. Natl. Acad. Sci. U.S.A.

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Hydropathic anticomplementarity of amino acids indicates that peptides derived from complementary DNA strands may form amphiphilic structures and bind one another. By using this concept, we have found that the antisense peptide Ser-Tyr-Asp-Leu complementary to the segment GlnIle-Val-Ala-Gly (residues 55-59) in cystatin C (an inhibitor of cysteine proteases) is located at positions 611-614 of the 18 chain of human C4, the fourth component of complement. Here we describe and characterize the specific interaction between cystatin C and C4 by ligand affinity chromatography and ELISA. Interaction between the two native proteins was mimicked on replacement of one of them with the corresponding sense-antisense peptide coupled to a carrier protein, and the binding was inhibited by these synthetic peptides in solution. Through the interaction with C4, cystatin C may play a regulatory role in complement activation that might be of particular importance at tissue sites where both proteins are produced by macrophages.Human cystatin C (formerly y trace) (1) is a basic protein of known primary structure (2) fully distributed in body fluids in a wide concentration range. It has been localized immunocytochemically in some cortical neurons, LH cells of the adenohypophysis, pancreatic A and thyroid C cells, and adrenal medulla (3). It is secreted into tissue culture medium by monocytes and other cells, and the down-regulation of its secretion may play a role in inflammation (4).Structural and genetic studies indicate that cystatin C is part of a superfamily that comprises three families, types I, II, and III (5,6). Type I cystatins (also called stefins) are proteins of "100 residues with no disulfide bonds. Type II cystatins (family that includes cystatin C) are molecules of 115-120 amino acids with two disulfide loops near the C terminus. Type III cystatins (kininogens) are high molecular weight proteins (Mr 68,000-110,000) composed of three cystatin type II-like domains (about 360 residues), the bradykinin moiety (9 amino acids), and a C-terminal polypeptide of variable length.Cystatins possess inhibitory activity against a broad spectrum of cysteine proteinases of plant origin (papain, chymopapain, ficin, and actinidin) as well as mammalian lysosomal proteases such as cathepsins B, H, and L (for review, see ref.7). The active site of inhibitory activity remains unknown, although some evidence suggests involvement of glycine at position 11 (8) and the segment 55-59 (cystatin C numbering) (6, 9, 10), both highly conserved in all known cystatins (7). Moreover, peptide Leu-Val-Gly (positions 9-11) inhibits growth of many bacteria, especially all group A streptococci, apparently due to inhibition of a cysteine protease produced by the bacteria (11).In addition to the inhibitory activity, the above-mentioned residues (almost identical in all members of the cystatin superfamily) may also be involved in protein-protein interactions. It is known that there is a tendency in the genetic code for codons of hydrophilic amino acids ...

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“…The main location of cystatin S is the salivary gland, but in human it has also been found in seminal vesicles (Abrahamson et al, 1986;Minakata et al, 1987;Shaw and Barka, 1989). The highest concentration of cystatin C so far described is in human semen (Grubb et al, 1983). Subsequent studies have shown that there is cystatin C mRNA in the testis, epididymis, prostate and seminal vesicles of the rat (Cole et al, 1989) and in human seminal vesicles (Abrahamson et al, 1990).…”

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confidence: 98%

Interactions between Ovine Cathepsin L, Cystatin C and α₂‐Macroglobulin — Potential Role in The Genital Tract

Peloille

Esnard

Dacheux

et al. 1997

European Journal of Biochemistry

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The specific inhibitor of cysteine proteinases, cystatin C, was purified from ram rete testis fluid and the conditioned medium of Sertoli cells. This molecule associated with sheep liver cathepsin L at one of the fastest rates ever described for a proteinasehnhibitor interaction (1.75 ?0.20X108 M-' . s-'). But the association rate constant for the interaction of cathepsin L with a,-macroglobulin, a nonspecific inhibitor of proteinases, was also extremely high (8.8-C0.75X106 M-' . s-I). Cathepsin L complexed with a,-macroglobulin was protected from inhibition by type 2 and type 3 cystatins. The data indicate that cystatin C is the most potent inhibitor of cathepsin L in mammalian male genital tract fluids, whereas a,-macroglobulin may act as a terminal acceptor of this enzyme. These inhibitors could therefore inhibit the activated form of procathepsin L which may appear during the complex process of spermatozoa production and maturation in the testis and epididymis.

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The γ-trace concentration of normal human seminal plasma is thirty-six times that of normal human blood plasma

Cited by 13 publications

References 13 publications

Molecular cloning and sequence analysis of cDNA coding for the precursor of the human cysteine proteinase inhibitor cystatin C

Molecular cloning and sequence analysis of cDNA coding for the precursor of the human cysteine proteinase inhibitor cystatin C

Binding of cystatin C to C4: the importance of sense-antisense peptides in their interaction.

Interactions between Ovine Cathepsin L, Cystatin C and α₂‐Macroglobulin — Potential Role in The Genital Tract

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The γ-trace concentration of normal human seminal plasma is thirty-six times that of normal human blood plasma

Cited by 13 publications

References 13 publications

Molecular cloning and sequence analysis of cDNA coding for the precursor of the human cysteine proteinase inhibitor cystatin C

Molecular cloning and sequence analysis of cDNA coding for the precursor of the human cysteine proteinase inhibitor cystatin C

Binding of cystatin C to C4: the importance of sense-antisense peptides in their interaction.

Interactions between Ovine Cathepsin L, Cystatin C and α2‐Macroglobulin — Potential Role in The Genital Tract

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Interactions between Ovine Cathepsin L, Cystatin C and α₂‐Macroglobulin — Potential Role in The Genital Tract