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Protein Absorption J Clin Pathol: first published as 10.1136/jcp.s3-5.1.29 on 1 January 1971. Downloaded from J. clin. Path., 24, Suppl. (Roy. Coll. Path.), 5, 29-40 Proteins Protein absorption D. M. MATTHEWS From the Department of Chemical Pathology, Westminster Medical School, London In the last 20 years, the mechanisms of protein epithelial cells. Small amounts of plasma proteins absorption have been studied with increasing in- (1-2 g) also enter the gastrointestinal lumen. The tensity, and a large book could be written on this sum of protein entering the gut may thus be not subject alone. In spite of this volume of work, it has much less than the dietary intake. This is one of recently become clear that our knowledge of protein many reasons why the pattern of amino acids appear- absorption is still far from complete, since until very ing in the portal or peripheral blood after ingestion recently nearly all investigations have been concerned of a certain protein reflects only rather indefinitely with the intestinal transport of amino acids. Evid- the composition of the protein fed. ence for the existence of a second important mode There is no reasonable doubt that in man most of of protein absorption-mucosal uptake of small the ingested protein is absorbed in the upper two- peptides with cellular hydrolysis-is now extremely thirds of the small intestine (Borgstrom, Dahlqvist, strong, and the importance of this mode of absorp- Lundh, and Sj6vall, 1957; Booth, 1968; Nixon and tion is maintaining nutrition in cases of intestinal Mawer, 1970a and b). Perfusion experiments in man copyright. transport defects for amino acids has recently been suggest that the absorptive capacity for neutral demonstrated. Yet the details of mucosal oligo- amino acids is higher in the jejunum than the ileum peptide transport have hardly begun to be explored. (Adibi, 1969). However, the absorptive capacity of It is therefore difficult to give a balanced account of the small intestine for protein digestion products is protein absorption at the present time. This account good throughout, and resections, unless very ex- is selective, most attention being paid to growing tensive, do not seriously impair protein absorption. points in the field. Several reviews covering the Mucosal dipeptidase activities are relatively low in details of amino-acid absorption are available the most proximal part of the human duodenum, http://jcp.bmj.com/ (Wilson, 1962; Wiseman, 1964; Matthews and becoming higher distally (Lindberg, 1966); in the Laster, 1965; Saunders and Isselbacher, 1966; Fisher, rat, they are maximal in the ileum (Robinson and 1967; Wiseman, 1968; Matthews, 1969) and will Shaw, 1960). In the rat, absorption from high con- supply references not given in the present text. centrations of a dipeptide (L-methionyl-L-methio- nine) was greater in the jejunum than in the lower General Considerations ileum (M. T. Lis, R. F. Crampton, and D. M. Matthews, unpublished data). Absorption of protein on September 27, 2021 by guest. Protected Protein absorption, like the absorption of fat and digestion products is mainly into the portal blood. carbohydrate, is normally a highly effective process, net absorption in man amounting to about 90%. Protein Digestion Since much of the faecal nitrogen (totalling 1-2 g per day) is endogenous in origin, the proportion of Protein digestion is initiated by gastric proteinases ingested protein entering the body is probably (pepsins) with pH optima on the acid side of neu- higher than 90 %6-possibly 95 %. It has been trality; two or more such enzymes are distinguish- realized in recent years that a good deal of protein able in man and other animals (Taylor, 1968). While enters the gut daily in various forms, and that most gastric digestion of protein is fairly extensive in the of this is digested and re-absorbed along with mechanical sense, it is unlikely that it proceeds in ingested protein. According to one of the more vivo beyond the stage of producing a mixture of conservative estimates (Munro, 1966), the protein large polypeptides and unaltered protein. The content of secretions into the human gut (digestive release of free amino acids may well be negligible. enzymes and mucus) amounts to 20-30 g per day, and Gastric digestion of protein is relatively unimportant, another 30 g or more comes from desquamated and in pernicious anaemia, with its virtually total 29 2 J Clin Pathol: first published as 10.1136/jcp.s3-5.1.29 on 1 January 1971. Downloaded from 30 D. M. Matthews failure of acid and pepsinogen secretion, there is no Jesuitova, Timofeeva, and Chernjahovskaja, 1967) evidence that protein absorption is impaired. is an attractive one, but here we are entering a Protein digestion is, in fact, very readily initiated by controversial area. There are a number of oligo- pancreatic proteolytic enzymes, without any pre- peptidases (peptidases hydrolysing peptides consist- liminary exposure to pepsin. It is of interest that the ing of a few amino-acid units) in the intestinal source of much popular lore about the digestibility mucosa, including several dipeptidases. Knowledge or indigestibility of various foodstuffs is research of these enzymes and their subcellular location is carried out in the 19th century on the rapidity of still very incomplete. While some, including an peptic digestion (Ewald, 1891). enzyme which cleaves amino acids sequentially from Once proteins and the products of peptic digestion oligopeptides of some six amino-acid units, may be have left the stomach and are exposed to the pro- situated at least partially in the brush border, there is teolytic enzymes of the pancreas, chemical break- evidence that others are largely located within down is extensive and extremely rapid. The pan- mucosal cells (Lindberg, 1966; Rhodes, 1968; Peters, creatic phase of protein digestion is of great import- 1970). This, in conjunction with transport studies ance. The pancreatic proteases, which have pH (below), makes it most unlikely that the terminal optima close to the pH of the duodenal contents stages of protein digestion are entirely superficial. (about 6 5), are all secreted in the form of inactive precursors. Activation is initiated by enterokinase, The Forms in which Proteins are Absorbed an enzyme produced by the intestinal mucosa, which converts trypsinogen to trypsin. Trypsin then con- Whole proteins are not absorbed in the adult animal verts the other enzyme precursors to their active except on a very small scale. The occurrence of this forms, and also acts autocatalytically to produce in man is suggested by the allergic reactions shown further activation of trypsinogen. Enterokinase is by some individuals to certain foodstuffs. In new- believed to be an enzyme of the brush border of the born animals, there is extensive absorption of whole intestinal mucosal cells (Nordstrom and Dahlqvist, proteins from milk, including maternal antibodies. cases have been in which It occurs by pinocytosis-the invagination of the 1970). Recently, reported copyright. congenital deficiency of enterokinase was respon- cell membrane to form minute vesicles (Clark, 1965). sible for apparent pancreatic insufficiency in infancy The question to be discussed here is that of the (Tarlow, Hadorn, Arthurton, and Lloyd, 1970a). form or forms in which protein is absorbed in the The pancreatic proteases may be divided into (1) adult mammal. In the latter part of the 19th century, endopeptidases, such as trypsin and chymotrypsin, it was widely believed that proteins were absorbed which attack peptide bonds located within the as polypeptides, but following the demonstration amino-acid chains of proteins and polypeptides, by Cohnheim in 1901 that there was peptidase breaking them into smaller fragments; and (2) activity ('erepsin') in the 'succus entericus' (fluid http://jcp.bmj.com/ exopeptidases, such as carboxypeptidases A and B, collected from the intestinal lumen) it gradually which cleave the terminal bonds of proteins or became accepted that proteins were completely peptides, splitting off amino acids. Study of cleavage hydrolysed to amino acids in the intestinal lumen sites suggests that the endo- and exopeptidases act before absorption, and then absorbed by diffusion. in concert, the action of endopeptidases producing This became the classical view of protein absorption peptide substrates suitable for further breakdown (eg, Verz'ar and McDougall, 1936). In the years by exopeptidases (Keller, 1968). The result, as before 1914, several investigators reported that on September 27, 2021 by guest. Protected judged from analyses of luminal contents, is produc- 'peptones' produced by tryptic hydrolysis of protein tion of a complex mixture of oligopeptides (prob- disappeared from the intestinal lumen more rapidly ably predominantly composed of 2-6 amino-acid than amino acids (Messerli, 1913; Verzar and units) and free amino acids. Further breakdown of McDougall, 1936), which seemed to suggest that the oligopeptides is brought about by the peptidases some protein at least might be absorbed as peptides, of the intestinal mucosa. Reports of the binding of but as the classical view of protein absorption pancreatic proteases to the brush border (Goldberg, hardened, these claims were regarded with scepticism Campbell, and Roy, 1969; Woodley and Kenny, or ignored. In fact, by 1935, this view had become so 1969) suggest the possibility that much protein diges- firmly established that Heath and Fullerton (1935), tion occurs in this region and that intralumen and whose results in man suggested to them that 'membrane digestion' (Ugolev, 1965 and 1968) may 'peptone' was absorbed more rapidly than the same not be clearly distinguishable. The concept that quantity of glycine, stated that their data could not adsorbed pancreatic proteases might act in conjunc- be interpreted in this way, because the peptone tion with superficially placed mucosal peptidases to 'containing mostly larger molecules than glycine, complete the process of protein digestion (Ugolev, should theoretically be absorbed more slowly'.
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