A crystalline trypsine inhibitor from swine colostrum

Laskowski, M.; Kassell, Beatrice; Hagerty, G.

doi:10.1016/0006-3002(57)90198-1

Cited by 77 publications

(53 citation statements)

References 9 publications

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“…One ml of the 1st-day colostrum from the pig inhibits about 2000 pg and from the cow about 600 pg of trypsin, whereas the corresponding figure for human milk from the first 3 days is 20-60 pg (2,17,21,22). Laskowski and Laskowski (22) could not detect any inhibitor on the 5th day, and Hyanek et al (17) reported low values (0-20 pg) on the 6th day. The present study obtained somewhat higher values.…”

Section: Time After Deliverymentioning

confidence: 94%

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Protease Inhibitors in Human Milk

Lindberg

1979

Pediatr Res

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Summarystandard serum for the measurements of the concentration of a,-Protease inhibitors (inhibiting trypsin, chymotrypsin, and elastase) were demonstrated in human milk from birth to 4 months after delivery. No pepsin inhibitor was found. The protease inhibitors were localized in the al-region-inhibiting trypsin, chymotrypsin, and elastase-and in a more cathodal region-inhibiting chymotrypsin-in agarose gel electrophoresis of human milk. alantitrypsin and antichymotrypsin were demonstrated by crossed immunoelectrophoresis. Electroimmunoassay showed the concentration of a,-antitrypsin in 1st day milk to be 109% and the concentration of antichymotrypsin was 116% of that of adult serum. The concentrations d&;eased during the 1st wk; from 1 wk to 4 months they were 1.6% for a,-antitrypsin and 3.84% for antichymotrypsin of those of adult serum. One ml of human milk from the first 3 days inhibits, by enzymatic methods, 0-150 pg (mean value, 70 pg) trypsin. Milk from 1 week after delivery and later inhibits 0-65 pg (mean value, 38 pg) trypsin per ml.

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Section: Time After Deliverymentioning

confidence: 94%

“…Trypsin inhibitor in human and bovine colostrum was demonstrated in 1951 by Laskowski & Laskowski (22). The bovine colostral trypsin inhibitor was later isolated and characterized, and isoinhibitors have been demonstrated (2,9,10,19,27).…”

mentioning

confidence: 99%

Protease Inhibitors in Human Milk

Lindberg

1979

Pediatr Res

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“…Secondly, colostral IgG 1 , in the cow at least, is more resistant to proteolysis by chymotrypsin than are other immunoglobulin classes (Brock et al 1977a(Brock et al , 1977b. Thirdly, colostrum contains a substance known as 'trypsin inhibitor' which prevents trypsin-mediated proteolysis ofthe immunoglobulin (Laskowski and Laskowski 1951;Balfour and Comline 1962). Additional absorption-enhancing factors must be involved, however, since the absorption of polyvinyl pyrollidone, which is not susceptible to enzymatic digestion, is enhanced if it is fed together with colostrum (Hardy 1964).…”

Section: Mammary Secretion As a Source Of Circulating Passively Acqumentioning

confidence: 99%

Immunological Functions of the Mammary Gland and Its Secretion-Comparative Review

Dl¹

1980

Aust. Jnl. Of Bio. Sci.

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The mammary gland performs vitally important immunological roles, both in providing passive immune protection to the suckling infant and in immunological defence of its own tissues against infection with microorganisms. These immunological functions differ greatly between species of mammals in both nature and magnitude. In ungulates the mammary gland is singularly responsible for transfer of immunoglobulin (IgG) from mother to young. This process is dependent on a highly selective mechanism which results in the transport of blood-borne IgG molecules across secretory epithelial cells of the colostrum-forming mammary gland and into secretion. Upon ingestion of colostrum by the young ungulate this immunoglobulin is absorbed across the wall of the small intestine and thence into the bloodstream.In other species, including rodents and primates, there is a well-developed local IgA system operating in the mammary gland. In this situation, plasma cells located near the basal membranes of secretory epithelial cells secrete IgA which passes through the epithelial cells and into colostrum or milk. In these species the IgA in mammary secretions is not absorbed into the circulation of the suckling infant; because of its unique property of resisting proteolytic degradation, it may mediate a local protective role in the lumen of the intestine of the suckling infant.Specific immunological protection of mammary tissue may be mediated through blood-derived antibody (particularly IgG), locally synthesized antibody (particularly IgA) or phagocytic cells. Neutrophils arrive in mammary tissue and secretions in very large numbers following bacterial invasion of the gland. It has been established recently that these cells carry cytophilic antibody on their cell membrane. This cytophilic antibody can play an important functional role in enhancing the phagocytic capacity of neutrophils in the mammary gland.

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“…H M G F 111 was given to mice subcutaneously rather than orally because subcutaneous administration is a much more efficient technique for growth factor delivery. However, the resistance of HMGF 111 to inactivation by HCI, pH 1 (3), and the presence of trypsin inhibitors in human milk (25) make it plausible that this growth factor could survive passage through the gastrointestinal tract. Thus the antiulcer effect of H M G F I11 might be one of the protective mechanisms that human milk is postulated to have for the breast-fed infant.…”

Section: Resultsmentioning

confidence: 99%

Human Milk-Derived Growth Factor Prevents Duodenal Ulcer Formation

1985

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ABSTRACT. Human milk was fractionated to obtain a MATERIALS AND METHODSpartially purified growth factor preparation. The growth factor in this fraction, designated as human milk growth factor 111, exhibits chromatographic and biological characteristics similar to epidermal growth factor-urogastrone. Pretreatment of mice with human milk growth factor I11 significantly reduces the incidence, number, total length, and severity score of cysteamine-induced duodenal ulcers. (Pediatr Res 19: 916-918, 1985) Abbreviations HMGF, human milk growth factor EGF, epidermal growth factor Human milk is a source of growth factor activity (1) and contains at least three species of growth factors (2). The predominant one. designated as HMGF 111, accounts for about 75% of the total growth factor activity in milk and is an acid-stable polypeptide with a mol wt of about 6000 and an isoelectric point of between 4.4 and 4.7 (2-4). These structural characteristics, along with Carpenter's (5) finding that about 70% of the growth factor activity in human milk can be neutralized by antibody directed against human EGF, strongly suggest that EGF or a closely related polypeptide is the major growth factor in human milk. EGF, a polypeptide first isolated from submaxillary glands (6), was found to bc structurally similar to urogastrone, a polypeptide prepared from urine (7). EGF-urogastrone is a potent mitogen for a variety of cells (8) and is known to stimulate the growth and maturation of the intestinal mucosa (9, 10). Besides being a mitogen, EGF-urogastrone is an inhibitor of gastric acid secretion (1 1) and has been used to promote healing of ulcers (12). Moreover, EGF-urogastrone has been localized by immunostaining in the duodenal (Brunner's) glands (1 3, 14). Specific receptors for EGF-urogastrone have been demonstrated in intestinal epithelial cells (15). Such findings suggest that EGFurogastrone plays a role in the secretion and growth of the gastrointestinal tract. Recently, Kirkegaard et al. (16) reported that EGF significantly inhibits the formation of cysteamineinduced duodenal ulcer in the rat. A similar activity in human milk would be of physiological interest since it would suggest that defined macro-molecular factors in human milk are capable of having an effect on the gastrointestinal tract of the human infant. This report demonstrates that a partially purified HMGF 111 is capable of protecting mice against the formation of duodenal ulcers induced by cysteamine in a dose-dependent manner. Human milk was kindly provided by Dr. Cutberto Garza of the Baylor College of Medicine, Houston, TX. HMGF 111 was prepared as previously described (2). In brief, about 100 ml of human milk was centrifuged at 13,000 x g for 60 min at 4" C. The fat at the top of the centrifuge tube and the cells and debris at the bottom were discarded. The skimmed milk was acidified by adjusting the pH to 4.3 with HCI and centrifuged at 30,000 x g for 60 min to remove precipitate. The supernatant fraction, which contained about 1.5 g of protein determined by...

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A crystalline trypsine inhibitor from swine colostrum

Cited by 77 publications

References 9 publications

Protease Inhibitors in Human Milk

Protease Inhibitors in Human Milk

Immunological Functions of the Mammary Gland and Its Secretion-Comparative Review

Human Milk-Derived Growth Factor Prevents Duodenal Ulcer Formation

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