Transglutaminases in mammalian reproductive tissues and fluids: relation to polyamine metabolism and semen coagulation

Williams-Ashman, H.G.; Beil, Richard E.; Wilson, J. H. P.; Hawkins, M.; Grayhack, John T.; Zunamon, A.; Weinstein, N.K.

doi:10.1016/0065-2571(80)90018-7

Cited by 66 publications

(17 citation statements)

References 24 publications

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“…They are secreted in plasma [4,25,301 and seminal fluid [51], expressed as soluble intracellular enzymes in peripheralblood cells [13, 361, lens [26], epidermis [5, 321, hair follicles [9,201, and numerous other tissues [8], and expressed as particulate enzymes in rat lung [lo, 191, lens [2], and liver [7,461, as well as in cell lines from various sources [3]. These types constitute a family of distinct enzymes, as judged by their biochemical properties [I61 and the regulation of their synthesis by physiological agents such as vitamin A, cyclic AMP, hydrocortisone, and calcium [13,24,42,491.…”

Section: Introductionmentioning

confidence: 99%

Induction of keratinocyte type-I transglutaminase in epithelial cells of the rat

1986

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Abstract. Using immunogold-silver techniques, we have demonstrated that, in rats, type-I (keratinocyte) transglutaminase is expressed primarily in stratified squamous epithelia of the integument. the upper digestive tract, and the lower female genital tract. In these epithelia, the enzyme was found to be present predominantly in the granular layer, but was evident at low levcls even in the basal layer, especially in the genital tract. N o immunoreactivity was detected in glandular, columnar, or transitional epithelia or in soft tissues. However, considerable enzyme antigenicity was observed in the endometrium and in major ducts of the pancreas and mammary glands of near-term pregnant and early postpartum females. In cultures, substantial immunoreactivity was readily identifiable not only in epidermal, vaginal, and esophageal epithelial cells (immunopositive in vivo), but also in urinary bladder, seminal vesicle, and tracheal epithelial cells (immunonegative in vivo). Primary epithelial outgrowths from bladder and seminal vesicle tissue explants were immunopositive, demonstrating rapid adaptation to the culture environment. These results reveal three distinct levels of regulation of transglutaminase exprcssion in various cell types: (1 ) during the differentiation of keratinocytes, (2) during pregnancy, being evident principally in the endometrium but detectable elsewhere as well, and (3) during the cultivation of certain epithelia which do not normally express the cnzyme in vivo. We conclude that type-I transglutaminase may be a valuable marker for elucidating the regulation of normal epithelial differentiation and squamous metaplasia.

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Section: Introductionmentioning

confidence: 99%

Induction of keratinocyte type-I transglutaminase in epithelial cells of the rat

1986

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“…Within Culicidae, formation of a mating plug is specific to Anopheles (6). TG-mediated cross-linking of seminal fluid proteins occurs in rodents (7), but other invertebrates use different mechanisms, such as secretion of O-glycosylated mucins in Caenorhabditis elegans (8) and homopolymerization of PEBII in Drosophila melanogaster (9).…”

Section: Transglutaminases (Tgs)mentioning

confidence: 99%

Characterization of Anopheles gambiae Transglutaminase 3 (AgTG3) and Its Native Substrate Plugin

Nguyen

Logarajah

et al. 2013

Journal of Biological Chemistry

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Background:A. gambiae transglutaminase AgTG3 cross-links Plugin within seminal fluids. Results: AgTG3 and Plugin were purified and their structure and activity characterized in vitro. Conclusion: AgTG3 forms a dimer in solution, analogous to human FXIII. Plugin is nonglobular in solution. AgTG3 is Ca 2ϩ -dependent and prefers Plugin as a substrate. Significance: Inhibition of AgTG3 cross-linking of Plugin is a possible method to chemosterilize male Anopheles mosquitoes.

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“…The enzyme is known to be present in various tissues [1][2][3][4][5][6]. Recently, Bruce et al [7] sug gested that gliadin would be a suitable sub strate for this enzyme and postulated that TG in intestine may be important in binding gliadin.…”

Section: Introductionmentioning

confidence: 99%

Transglutaminase Activity along the Rat Small Bowel and Cellular Location

D’Argenio

Sorrentini²,

Ciacci³

et al. 1988

Enzyme

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A recent report indicates a relationship between human transglutaminase (TG) jejunal mucosa activity and celiac disease. We investigated the enzyme distribution along six consecutive small bowel segments of mucosa and tested TG activity on brush border membranes obtained from whole mucosa homogenate in Wistar rats. TG activity was significantly present in jejunal mucosa even if mostly detected in the distal part of small intestine. Our study indicates highest enzymatic activity in the subcellular fraction containing organelles and cellular membranes (66.8%) while a 7% activity was associated with the brush border fraction.

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Transglutaminases in mammalian reproductive tissues and fluids: relation to polyamine metabolism and semen coagulation

Cited by 66 publications

References 24 publications

Induction of keratinocyte type-I transglutaminase in epithelial cells of the rat

Induction of keratinocyte type-I transglutaminase in epithelial cells of the rat

Characterization of Anopheles gambiae Transglutaminase 3 (AgTG3) and Its Native Substrate Plugin

Transglutaminase Activity along the Rat Small Bowel and Cellular Location

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