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

Kubiak, Agnieszka; Jakimowicz, Piotr; Polanowski, Antoni

doi:10.1016/j.ijbiomac.2009.05.001

Cited by 5 publications

(2 citation statements)

References 43 publications

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“…ClTI-1/SPINK2 is a serine protease inhibitor that was previously identified in chicken liver and then found in chicken seminal plasma and (Kubiak et al, 2009;Labas et al, 2015;Lessley & Brown, 1978).…”

Section: Discussionmentioning

confidence: 99%

“…Using an experimental line of chicken, we recently identified a seminal protein, chicken liver trypsin inhibitor 1 (ClTI-1) that was present with variable abundance in semen of healthy roosters with contrasted fertility (Labas et al, 2015). This protein was previously purified from chicken liver and seminal plasma using a chromatography based on its trypsin inhibitor property (Kubiak, Jakimowicz, & Polanowski, 2009;Lessley & Brown, 1978) but its function as well as its target proteases remain unknown.…”

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confidence: 99%

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The seminal acrosin‐inhibitor ClTI1/SPINK2 is a fertility‐associated marker in the chicken

Thélie

Réhault-Godbert

Poirier

et al. 2019

Molecular Reproduction Devel

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The seminal plasma is a very complex fluid, which surrounds sperm in semen. It contains numerous proteins including proteases and protease inhibitors that regulate proteolytic processes associated with protein activation and degradation. We previously identified a seminal protein, chicken liver trypsin inhibitor 1 (ClTI‐1) over expressed in semen of roosters with high fertility, suggesting a role in male fertility. In the present study, we showed that ClTI‐1 gene is actually SPINK2. Using normal healthy adult roosters, we showed that SPINK2 amount in seminal plasma was positively correlated with male fertility in chicken lines with highly contrasted genetic backgrounds (broiler and layer lines). Using affinity chromatography combined to mass spectrometry analysis and kinetic assays, we demonstrated for the first time that two chicken acrosin isoforms (acrosin and acrosin‐like proteins) are the physiological serine protease targets of SPINK2 inhibitor. SPINK2 transcript was overexpressed all along the male tract, and the protein was present in the lumen as expected for secreted proteins. Altogether, these data emphasize the role of seminal SPINK2 Kazal‐type inhibitor as an important actor of fertility in birds through its inhibitory action on acrosin isoforms proteins.

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

The seminal acrosin‐inhibitor ClTI1/SPINK2 is a fertility‐associated marker in the chicken

Thélie

Réhault-Godbert

Poirier

et al. 2019

Molecular Reproduction Devel

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Natural and Engineered Plasmin Inhibitors: Applications and Design Strategies

Swedberg¹,

Harris²

2012

ChemBioChem

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The serine protease plasmin is ubiquitously expressed throughout the human body in the form of the zymogen plasminogen. Conversion to active plasmin occurs through enzymatic cleavage by plasminogen activators. The plasminogen activator/plasmin system has a well-established function in the removal of intravascular fibrin deposition through fibrinolysis and the inhibition of plasmin activity; this has found widespread clinical use in reducing perioperative bleeding. Increasing evidence also suggests diverse, although currently less defined, roles for plasmin in a number of physiological and pathological processes relating to extracellular matrix degradation, cell migration and tissue remodelling. In particular, dysregulation of plasmin has been linked to cancer invasion/metastasis and various chronic inflammatory conditions; this has prompted efforts to develop inhibitors of this protease. Although a number of plasmin inhibitors exist, they commonly suffer from poor potency and/or specificity of inhibition that either results in reduced efficacy or prevents clinical use. Consequently, there is a need for further development of high-affinity plasmin inhibitors that maintain selectivity over other serine proteases. This review summarises clearly defined and potential applications for plasmin inhibition. The properties of naturally occurring and engineered plasmin inhibitors are discussed in the context of current knowledge regarding plasmin structure, specificity and function. This includes design strategies to obtain the potency and specificity of inhibition in addition to controlled temporal and spatial distribution tailored for the intended use.

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Recent Advances on Plasmin Inhibitors for the Treatment of Fibrinolysis‐Related Disorders

Al‐Horani

Desai

2014

Medicinal Research Reviews

101

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Growing evidence suggests that plasmin is involved in a number of physiological processes in addition to its key role in fibrin cleavage. Plasmin inhibition is critical in preventing adverse consequences arising from plasmin overactivity, e.g., blood loss that may follow cardiac surgery. Aprotinin was widely used as an antifibrinolytic drug before its discontinuation in 2008. Tranexamic acid and ε-aminocaproic acid, two small molecule plasmin inhibitors, are currently used in the clinic. Several molecules have been designed utilizing covalent, but reversible, chemistry relying on reactive cyclohexanones, nitrile warheads, and reactive aldehyde peptidomimetics. Other major classes of plasmin inhibitors include the cyclic peptidomimetics and polypeptides of the Kunitz and Kazal-type. Allosteric inhibitors of plasmin have also been designed including small molecule lysine analogs that bind to plasmin's kringle domain(s) and sulfated glycosaminoglycan mimetics that bind to plasmin's catalytic domain. Plasmin inhibitors have also been explored for resolving other disease states including cell metastasis, cell proliferation, angiogenesis, and embryo implantation. This review highlights functional and structural aspects of plasmin inhibitors with the goal of advancing their design.

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

Cited by 5 publications

References 43 publications

The seminal acrosin‐inhibitor ClTI1/SPINK2 is a fertility‐associated marker in the chicken

The seminal acrosin‐inhibitor ClTI1/SPINK2 is a fertility‐associated marker in the chicken

Natural and Engineered Plasmin Inhibitors: Applications and Design Strategies

Recent Advances on Plasmin Inhibitors for the Treatment of Fibrinolysis‐Related Disorders

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