Transient Lubrication of an Accelerated Infinite Slider

Lyman, F. A.; Saibel, Edward

doi:10.1080/05698196108972424

Cited by 13 publications

(8 citation statements)

References 2 publications

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“…Furthermore, the time of maximal stimulation by PCI occlurs later, that is, between 4 and 8 hr after feeding the inhibitor; whereas when SBTI is fed, maximum stimulation is obtained between 2 and 6 hr. The data also indicate that the large increases in intestinal proteolytic activity previously observed when total proteolytic aativity was measured by hemoglobin digestion (1,8) in rats after SBTI was fed were due mainly to increased chymotrypsin activity, rather than to trypsin.…”

Section: And 6 Hrmentioning

confidence: 82%

“…4), the inhibition of either chymotrypsin or trypsin was suffiuenlt to elicit and maintain a pancreatic response. However, Lyman et al ( 1 ) have demonstrated that the feeding of a large excess of trypsin along with SBTI did not diminish the pancreatic response compared to rats fed SBTI alone. Under these conditions, one would not expect that a deficiency of intestinal trypsin wouljd occur, so the question of what triggers the secretion still remains unclear.…”

Section: And 6 Hrmentioning

confidence: 96%

“…An increase in pancreatic enzyme secretion and pancreatic hypertrophy following the ingestion of various trypsin inhibitors are well established phenomena in rats and chicks (1,2 ) . The diverse origins of the many trypsin inhibitolrs that elicit the pancreatic response-their dissimilarity in molecular weight, heat lability, and other physicochemical properities-suggest that their physiological effect, when fed to animals, must be related to their common property, the ability to inhibit tryptic hydrolysis.…”

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confidence: 98%

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Chymotrypsin Inhibitor Stimulation of Pancreatic Enzyme Secretion in the Rat

Green¹,

Lyman²

1971

Experimental Biology and Medicine

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An increase in pancreatic enzyme secretion and pancreatic hypertrophy following the ingestion of various trypsin inhibitors are well established phenomena in rats and chicks (1, 2 ) . The diverse origins of the many trypsin inhibitolrs that elicit the pancreatic response-their dissimilarity in molecular weight, heat lability, and other physicochemical properities-suggest that their physiological effect, when fed to animals, must be related to their common property, the ability to inhibit tryptic hydrolysis.No studies, to our knowledge, have been published which have described the pancreatic response to inhibitors of the other major pancreatic proteol y t ic enzyme, chymo tr ypsin. The reason for this lies probably in the fact that, until recently, no "pure" chymotrypsin inhibitor (i.e., one which is devoid of trypsin inhibitor or other enzyme inhibitor activity) suitable for dietary studies was available. With the discovery and isolation by Ryan and Balls ( 3 ) of a chymotrpin inhibitor from potatoes, such a study became feasible. The investigation described below compared the acute exocrine pancreatic response of rats fed a single dose of potato chymotrypsin inhibitor (PCI) to that of rats fed either soy bean trypsin inhibitor (SBTI) or the control diet containing casein. Materials and Methods.Male, Long-Evans rats weighing 90-1 10 g, were purchased from a local supplier (Simonsen, Gilroy, California) and were maintained ad libitum oa Purina Laboratory Rat Chow. Food was removed from the animals 24 hr before an experiment. In each experiment, the inhibitor or protein to be fed was mixed with 2 g of a basic, 18% casein semipurified diet contain-1 This investigation was supported in part by U S .Public Health Service Grant-in-Aid AM-3046.ing 71% sucrose and no celluflour (4) and with enough water to form a viscous slurry, which was then placed in the animal by stomach tube. The rats were divided into 4 groups: Group I received the basic diet plus 25 mg/100 g of body weight of PCI; group I1 was fed the diet plus 42 mg/100 g of body weight of SBTI; group 111, the control group, was fed the diet plus 50 mg/100 g of body weight of purified casein; group IV was not fed following the 24-hr fast, and was used to establish the fastin,g levels of the enzymes assayed. The quantities of the inhibitors fed in each case were identical in terms of the total amount of enzyme they inhibited (i.e., 25 mg of PCI and 42 mg of SBTI inhibited 42 mg of bovine a-chymotrypsin and 42 mg of bovine trypsin, respectively). The amount of SBTI fed was known from previous experience to be more than adequate to elicit a maximal response from the rat pancreas.Groups I, 11, and I11 were sacrificed by decapitation at 2, 4, 6, and 8 hr after receiving the diets by stomach-tube, and group IV was killed following the 24-hr fast. The pancreas and intestinal contents were immediately removed. The pancreas was dissected free of visible fat and lymph nodes under a dissecting microscope, frozen, and lyophilized. Intestinal contents were collected by dividi...

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Section: And 6 Hrmentioning

confidence: 82%

Section: And 6 Hrmentioning

confidence: 96%

mentioning

confidence: 98%

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Chymotrypsin Inhibitor Stimulation of Pancreatic Enzyme Secretion in the Rat

Green¹,

Lyman²

1971

Experimental Biology and Medicine

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“…1988; Lyman et al, 1988), confirming that the levels of tyrosine kinase necessary to induce cell transformation need not be optimal. Consistent with these observations, CSF-l stimulation of cells expressing CSF-lR[ser3Ol] led to an enhancement of their associated Ptdlns 3-kinase activity (Table I).…”

Section: Resultsmentioning

confidence: 99%

Structural features of the colony-stimulating factor 1 receptor that affect its association with phosphatidylinositol 3-kinase.

et al. 1990

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The colony‐stimulating factor 1 receptor (CSF‐1R), immunoprecipitated with either anti‐phosphotyrosine or anti‐receptor antibodies from lysates of ligand‐stimulated cells, is associated with a phosphatidylinositol (PtdIns) 3‐kinase activity. The ligand‐independent transforming efficiencies of human CSF‐1R mutants containing certain amino acid substitutions at codon 301 in their extracellular domains correlated directly with their levels of associated lipid kinase activity. A tyrosine kinase defective CSF‐1R mutant (CSF‐1R[met616]), containing a mutated ATP binding site, lacked associated PtdIns 3‐kinase activity in immune complexes recovered from CSF‐1‐stimulated cells. However, CSF‐1R[met616] associated with PtdIns 3‐kinase when phosphorylated in trans in CSF‐1‐stimulated cells coexpressing an enzymatically competent CSF‐1R tyrosine kinase. Another CSF‐1R mutant, (CSF‐1R[delta KI]), lacking 67 amino acids from its intracellular ‘kinase insert’ domain, exhibited a partially impaired ligand‐dependent mitogenic response and a significant reduction in its associated PtdIns 3‐kinase activity. Ligand‐stimulated CSF‐1R[delta KI] molecules contained levels of phosphotyrosine almost equivalent to wild‐type receptors, but were phosphorylated at different sites in vitro. Therefore, the association of CSF‐1R with active PtdIns 3‐kinase required the receptor tyrosine kinase activity, was triggered by receptor phosphorylation on tyrosine and, in this series of mutants, correlated with their mitogenic potential. Although the receptor KI domain strongly contributes to the association with PtdIns 3‐kinase, this region is not strictly essential for the interaction.

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“…On the other hand, Lyman et al (15) found that both egg white and lima bean trypsin inhibitor (LBTI) induced pancreatic secretion similar to that produced by the SBTT. After observing that inactivation of the inhibitors with trypsin prior to feeding did not change the pattern of this response, the above mentioned authors concluded that the physiological activity of these substances was closely associated with their trypsin inhibitor activity but that inactivation of endogenous trypsin in the small intestine seemed not be be necessary for the response.…”

mentioning

confidence: 99%

Exocrine Function of the Chick Pancreas as Affected by Dietary Soybean Meal and Carbohydrate

Borgo¹,

Salman²,

Pubols³

et al. 1968

Experimental Biology and Medicine

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Chicks develop an enlarged pancreas when fed unheated soybean meal. Autoclaving the meal destroys or inactivates the heat-labile component(s) which cause this effect on the pancreas ( 5 ) . Recent histological studies in our laboratory (24) have confirmed that this enlargement is due to hyperplasia of the pan-* Scientific Paper NO. 3066, College of Agriculture, Washington State University, Pullman ; Project 1533.

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Transient Lubrication of an Accelerated Infinite Slider

Cited by 13 publications

References 2 publications

Chymotrypsin Inhibitor Stimulation of Pancreatic Enzyme Secretion in the Rat

Chymotrypsin Inhibitor Stimulation of Pancreatic Enzyme Secretion in the Rat

Structural features of the colony-stimulating factor 1 receptor that affect its association with phosphatidylinositol 3-kinase.

Exocrine Function of the Chick Pancreas as Affected by Dietary Soybean Meal and Carbohydrate

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