The coagulation of insect hemolymph

Theopold, Ulrich; Li, Dongmei; Fabbri, Marco; Scherfer, Christoph; Schmidt, Otto

doi:10.1007/s00018-002-8428-4

Cited by 145 publications

(107 citation statements)

References 111 publications

Supporting

Mentioning

104

Contrasting

Order By: Relevance

“…As we mentioned above, breakage of the host cuticle in invertebrates immediately induces the clotting of blood and melanization at the injury site [16,17]. These two reactions are essential to limit the spread of microbes during systemic infection.…”

Section: Coagulation and Melanizationmentioning

confidence: 95%

How Drosophila combats microbial infection: a model to study innate immunity and host–pathogen interactions

Tzou

Gregorio

Lemaître

2002

Current Opinion in Microbiology

325

228

View full text Add to dashboard Cite

Section: Coagulation and Melanizationmentioning

confidence: 95%

How Drosophila combats microbial infection: a model to study innate immunity and host–pathogen interactions

Tzou

Gregorio

Lemaître

2002

Current Opinion in Microbiology

325

228

View full text Add to dashboard Cite

“…Additionally, all five Acp protease inhibitors are present in the mated female's uterus, where they could potentially regulate the proteolytic processing of seminal fluid proteins such as ovulin (Park and Wolfner 1995). All five also enter the female's circulatory system (Lung et al 2002;Ravi Ram et al 2005; K. Ravi Ram, J. L. Mueller and M. F. Wolfner, unpublished data) and thus have the opportunity to regulate extracellular proteolytic cascades within the mated female (reviewed in Theopold et al 2002;Leclerc and Reichhart 2004). D. melanogaster Acp protease inhibitor proteins may interact with the many proteases identified in the female reproductive tract (Swanson et al 2004) or with pro-teases whose transcript levels are modulated by mating Begun 2004, 2007;McGraw et al 2004;Mack et al 2006) and/or present in the seminal fluid (Mueller et al 2005).…”

mentioning

confidence: 99%

Targeted Gene Deletion and Phenotypic Analysis of the Drosophila melanogaster Seminal Fluid Protease Inhibitor Acp62F

et al. 2008

View full text Add to dashboard Cite

Internally fertilizing organisms transfer a complex assortment of seminal fluid proteins, a substantial fraction of which are proteolysis regulators. In mammals, some seminal protease inhibitors have been implicated in male infertility and these same molecular classes of protease inhibitors are also found in Drosophila seminal fluid. Here, we tested the reproductive functions of the Drosophila melanogaster seminal fluid protease inhibitor Acp62F by generating a precise deletion of the Acp62F gene. We did not detect a nonredundant function for Acp62F in modulating the egg laying, fertility, remating frequency, or life span of mated females. However, loss of Acp62F did alter a male's defensive sperm competitive ability, consistent with the localization of Acp62F to sperm storage organs. In addition, the processing of at least one seminal protein, the ovulation hormone ovulin, is slower in the absence of Acp62F.

show abstract

“…In crustaceans, although no proteolytic cascades are involved in the hemolymph coagulation, the coagulation also depends on the TGase-mediated cross-linking of specific plasma-clotting proteins (1,4). Insect hemolymph coagulation requires close interaction between plasma components and cellular components derived from hemocytes, resulting in the precipitation of an insoluble matrix (5). This precipitation leads to a soft clot, which is hardened through the activity of cross-linking enzymes.…”

mentioning

confidence: 99%

A Cysteine-rich Protein from an Arthropod Stabilizes Clotting Mesh and Immobilizes Bacteria at Injury Sites

Matsuda¹,

Osaki²,

Hashii³

et al. 2007

Journal of Biological Chemistry

View full text Add to dashboard Cite

Hemolymph coagulation in arthropods plays key roles in host defense, including sealing wounds to staunch bleeding and immobilizing invading microorganisms. We have previously reported that horseshoe crab transglutaminase (TGase) promotes cross-linking of a clotting protein (coagulin) with hemocyte-derived proteins (proxins), resulting in the formation of stable coagulin fibrils. Here we show that TGase also cross-links proxins to another hemocyte-derived protein named stablin. Stablin is a cysteine-rich protein of 131 residues. Surface plasmon resonance analysis revealed the specific interaction of stablin with proxin-1 at K d ‫؍‬ 4.0 ؋ 10 ؊9 M. Stablin was predominantly localized in the large granules of hemocytes and secreted by lipopolysaccharide-induced exocytosis. Interestingly, stablin bound to chitin at K d ‫؍‬ 1.5 ؋ 10 ؊8 M, as determined by using a quartz-crystal microbalance. Stablin also interacted with lipopolysaccharides and lipoteichoic acids and exhibited bacterial agglutinating activity against Gram-positive and -negative bacteria. Immunostaining showed that stablin is co-localized with coagulin in the clotting fibrils that effectively trap bacteria. Moreover, an anti-stablin antibody strongly inhibited the proper formation of the clotting fibrils. These data suggest that stablin promotes the formation of the clotting mesh and the immobilization of invading microbes at injury sites. In arthropods, the TGase-mediated cross-linking may play an important role in the initial stage of host defense, wound closure, and healing, as in the case of mammals.

show abstract

The coagulation of insect hemolymph

Cited by 145 publications

References 111 publications

How Drosophila combats microbial infection: a model to study innate immunity and host–pathogen interactions

How Drosophila combats microbial infection: a model to study innate immunity and host–pathogen interactions

Targeted Gene Deletion and Phenotypic Analysis of the Drosophila melanogaster Seminal Fluid Protease Inhibitor Acp62F

A Cysteine-rich Protein from an Arthropod Stabilizes Clotting Mesh and Immobilizes Bacteria at Injury Sites

Contact Info

Product

Resources

About