Purification and Properties of a Proteinase Inhibitor from Chicken Seminal Plasma1

Lessley, Bruce A.; Brown, K. W.

doi:10.1095/biolreprod19.1.223

Cited by 23 publications

(12 citation statements)

References 31 publications

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“…The kinetic constants K M (Michaelis constant), k cat (catalytic rate constant), and K M /k cat are also different for the two forms of chicken trypsin [15]. The data presented here suggest that clTI-1 looks very much like the chicken seminal plasma inhibitor reported by Lessley and Brown [10]. Both of them show almost identical amino acid composition and molecular weight and very similar inhibitory activity against trypsin and plasmin and do not affect chymotrypsin.…”

Section: Inhibitory Activitysupporting

confidence: 48%

“…These facts suggest that PSTI may play an important role in host defence. The other members of the Kazal family are trypsin and acrosin inhibitors isolated from male reproductive tracts of mammals [8,9] and birds [10,11]. Their main postulated physiological function is the protection of reproductive tissues, seminal plasma proteins, and spermatozoa from the proteolytic action of acrosin liberated from the acrosomes of dead and damaged spermatozoa [1,10].…”

Section: Introductionmentioning

confidence: 99%

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A Kazal-type serine proteinase inhibitor from chicken liver (clTI-1)

Kubiak

Jakimowicz

Polanowski

2009

International Journal of Biological Macromolecules

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Section: Inhibitory Activitysupporting

confidence: 48%

Section: Introductionmentioning

confidence: 99%

A Kazal-type serine proteinase inhibitor from chicken liver (clTI-1)

Kubiak

Jakimowicz

Polanowski

2009

International Journal of Biological Macromolecules

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“…Proteolysis regulators are a component of the seminal fluid of many animal taxa, including insects and other invertebrates [1]–[7], fish [8]–[10], birds [11], [12], and mammals [13]–[18]. However, the mechanisms by which seminal proteases act, and most of the processes they affect, in mated females are poorly understood.…”

Section: Introductionmentioning

confidence: 99%

The Drosophila melanogaster Seminal Fluid Protease “Seminase” Regulates Proteolytic and Post-Mating Reproductive Processes

2012

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Proteases and protease inhibitors have been identified in the ejaculates of animal taxa ranging from invertebrates to mammals and form a major protein class among Drosophila melanogaster seminal fluid proteins (SFPs). Other than a single protease cascade in mammals that regulates seminal clot liquefaction, no proteolytic cascades (i.e. pathways with at least two proteases acting in sequence) have been identified in seminal fluids. In Drosophila, SFPs are transferred to females during mating and, together with sperm, are necessary for the many post-mating responses elicited in females. Though several SFPs are proteolytically cleaved either during or after mating, virtually nothing is known about the proteases involved in these cleavage events or the physiological consequences of proteolytic activity in the seminal fluid on the female. Here, we present evidence that a protease cascade acts in the seminal fluid of Drosophila during and after mating. Using RNAi to knock down expression of the SFP CG10586, a predicted serine protease, we show that it acts upstream of the SFP CG11864, a predicted astacin protease, to process SFPs involved in ovulation and sperm entry into storage. We also show that knockdown of CG10586 leads to lower levels of egg laying, higher rates of sexual receptivity to subsequent males, and abnormal sperm usage patterns, processes that are independent of CG11864. The long-term phenotypes of females mated to CG10586 knockdown males are similar to those of females that fail to store sex peptide, an important elicitor of long-term post-mating responses, and indicate a role for CG10586 in regulating sex peptide. These results point to an important role for proteolysis among insect SFPs and suggest that protease cascades may be a mechanism for precise temporal regulation of multiple post-mating responses in females.

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“…Proteolytic activity has been detected in chicken seminal plasma at acid or neutral pH [6][7], but no significant activity has been detected at basic pH [7][8][9]. In fact, chicken seminal plasma contains inhibitors of spermatozoal acrosin [10], a serine protease with optimum activity between pH 8 and 9 [5,[11][12][13].…”

Section: Introductionmentioning

confidence: 99%

Proteolytic Enzymes in Seminal Plasma of Domestic Turkey (Meleagris Gallopavo)1

Thurston

Korn

Froman

et al. 1993

Biology of Reproduction

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Protease and basic amidase activity was found in the seminal plasma of the domestic turkey. Amidase activity, measured through use of N-alpha-benzoyl-DL-arginine-p-nitroanilide-HCL (BAPNA), was 23-28 times greater for turkey than for guinea fowl or chicken. Within the reproductive tract, seminal plasma from the vas deferens had much greater activity than testicular or epididymal fluids. Turkey seminal plasma enzyme (TSPE) purified by chromatography or isoelectric focusing showed three protein bands by PAGE, each resolving on SDS-PAGE into two subunits with molecular weights of approximately 28,000-32,000 and 38,000-44,000. One of the three proteins also contained a larger subunit (M(r) 76,000-81,000) thought to be transferrin. Turkey acrosin consisted of three subunits with molecular weights below 20,500. Acrosin, but not TSPE, was visualized in native gels with N-alpha-benzoyl-DL-arginine-beta-naphthylamide (BANA)/Fast Garnet stain. Michaelis constants (BAPNA) for TSPE, acrosin, and trypsin were 2.41 +/- 0.12 x 10(-4) M (n = 5), 4.96-6.03 x 10(-4) M (n = 2), and 6.76 +/- 0.95 x 10(-4) M (n = 6), respectively. TSPE, like acrosin and trypsin, was inhibited by benzamidine but not iodoacetamide. While all natural trypsin inhibitors tested inhibited acrosin, TSPE was not inhibited by ovomucoid from chicken or turkey egg white.

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Purification and Properties of a Proteinase Inhibitor from Chicken Seminal Plasma1

Cited by 23 publications

References 31 publications

A Kazal-type serine proteinase inhibitor from chicken liver (clTI-1)

A Kazal-type serine proteinase inhibitor from chicken liver (clTI-1)

The Drosophila melanogaster Seminal Fluid Protease “Seminase” Regulates Proteolytic and Post-Mating Reproductive Processes

Proteolytic Enzymes in Seminal Plasma of Domestic Turkey (Meleagris Gallopavo)1

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