Stimulation of CCK and GLP-1 secretion and expression in STC-1 cells by human jejunal contents and in vitro gastrointestinal digests from casein and whey proteins

This study entails the possible interactions between whey protein and cranberry juice after processing, impacting either the protein digestibility or the bioaccessibility of cranberry antioxidants using an in vitro gastrointestinal digestion model.

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Comparison of the ability to bind lipids of β-lactoglobulin and serum albumin of milk from ruminant and non-ruminant species

Journal of Dairy Research ◽

10.1017/s0022029900027345 ◽

1993 ◽

Vol 60 (1) ◽

pp. 55-63 ◽

Cited By ~ 30

Author(s):

M. Dolores Pérez ◽

Pilar Puyol ◽

José Manuel Ena ◽

Miguel Calvo

Keyword(s):

Fatty Acids ◽

Guinea Pig ◽

Serum Albumin ◽

Whey Protein ◽

Whey Proteins ◽

Gel Filtration ◽

Ruminant Species ◽

Β Lactoglobulin

SummaryThe interaction of sheep, horse, pig, human and guinea-pig whey proteins with fatty acids has been studied. Using gel filtration and autoradiography, it was found that sheep β-lactoglobulin and serum albumin from all species had the ability to bind fatty acids in vitro. Sheep β-lactoglobulin, isolated from milk, had ˜ 0·5 mol fatty acids bound per mol monomer protein, and albumin from sheep, horse and pig contained ˜ 4·5, 2·9 and 4·7 mol fatty acids/mol protein respectively. However, β-lactoglobulin from horse and pig milk had neither fatty acids physiologically bound nor the ability to bind them in vitro. Albumin was the only whey protein detected with bound fatty acids in these species as well as in human and guinea pig. This suggests that the ability of ruminant β-lactoglobulin to bind fatty acids was not shared by the same protein of non-ruminants.

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Effect of Gel Structure on the In Vitro Gastrointestinal Digestion Behaviour of Whey Protein Emulsion Gels and the Bioaccessibility of Capsaicinoids

Molecules ◽

10.3390/molecules26051379 ◽

2021 ◽

Vol 26 (5) ◽

pp. 1379

Author(s):

Nan Luo ◽

Aiqian Ye ◽

Frances M. Wolber ◽

Harjinder Singh

Keyword(s):

Whey Protein ◽

Whey Proteins ◽

Micelle Formation ◽

Protein Isolate ◽

Gastric Digestion ◽

Lipid Digestion ◽

Gel Structure ◽

Oil Droplet ◽

Mechanical Strengths

This study investigated the effect of gel structure on the digestion of heat-set whey protein emulsion gels containing capsaicinoids (CAP), including the bioaccessibility of CAP. Upon heat treatment at 90 °C, whey protein emulsion gels containing CAP (10 wt% whey protein isolate, 20 wt% soybean oil, 0.02 wt% CAP) with different structures and gel mechanical strengths were formed by varying ionic strength. The hard gel (i.e., oil droplet size d4,3 ~ 0.5 µm, 200 mM NaCl), with compact particulate gel structure, led to slower disintegration of the gel particles and slower hydrolysis of the whey proteins during gastric digestion compared with the soft gel (i.e., d4,3 ~ 0.5 µm, 10 mM NaCl). The oil droplets started to coalesce after 60 min of gastric digestion in the soft gel, whereas minor oil droplet coalescence was observed for the hard gel at the end of the gastric digestion. In general, during intestinal digestion, the gastric digesta from the hard gel was disintegrated more slowly than that from the soft gel. A power-law fit between the bioaccessibility of CAP (Y) and the extent of lipid digestion (X) was established: Y = 49.2 × (X – 305.3)0.104, with R2 = 0.84. A greater extent of lipid digestion would lead to greater release of CAP from the food matrix; also, more lipolytic products would be produced and would participate in micelle formation, which would help to solubilize the released CAP and therefore result in their higher bioaccessibility.

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Early Platelet-Collagen Interactions in Whole Blood and Their Modifications by Aspirin and Dipyridamole Evaluated by a New Method (Basic Wave)

Thrombosis and Haemostasis ◽

10.1055/s-0038-1660136 ◽

1985 ◽

Vol 54 (04) ◽

pp. 799-803 ◽

Cited By ~ 14

Author(s):

José Luís Pérez-Requejo ◽

Justo Aznar ◽

M Teresa Santos ◽

Juana Vallés

Keyword(s):

Whole Blood ◽

Ex Vivo ◽

Platelet Rich Plasma ◽

White Blood Cells ◽

Reversible Aggregation ◽

Inhibitory Compounds ◽

Rapid Generation ◽

Stimulation Of ◽

Collagen Stimulation

SummaryIt is shown that the supernatant of unstirred whole blood at 37° C, stimulated by 1 μg/ml of collagen for 10 sec, produces a rapid generation of pro and antiaggregatory compounds with a final proaggregatory activity which can be detected for more than 60 min on a platelet rich plasma (PRP) by turbidometric aggregometry. A reversible aggregation wave that we have called BASIC wave (for Blood Aggregation Stimulatory and Inhibitory Compounds) is recorded. The collagen stimulation of unstirred PRP produces a similar but smaller BASIC wave. BASIC’s intensity increases if erythrocytes are added to PRP but decreases if white blood cells are added instead. Aspirin abolishes “ex vivo” the ability of whole blood and PRP to generate BASIC waves and dipyridamole “in vitro” significantly reduces BASIC’s intensity in whole blood in every tested sample, but shows little effect in PRP.

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DER EINFLUSS VON RESERPIN AUF DIE ANTITHYREOIDALE WIRKUNG VON KALIUMPERCHLORAT

Acta Endocrinologica ◽

10.1530/acta.0.0390423 ◽

1962 ◽

Vol 39 (3) ◽

pp. 423-430

Author(s):

H. L. Krüskemper ◽

F. J. Kessler ◽

E. Steinkrüger

Keyword(s):

Thyroid Gland ◽

Male Rats ◽

Normal Male ◽

Tissue Respiration ◽

List Type ◽

Morphological Alterations ◽

Hormone Synthesis ◽

Stimulation Of

ABSTRACT 1. Reserpine does not inhibit the tissue respiration of liver in normal male rats (in vitro). 2. The decrease of tissue respiration of the liver with simultaneous morphological stimulation of the thyroid gland after long administration of reserpine is due to a minute inhibition of the hormone synthesis in the thyroid gland. 3. The morphological alterations of the thyroid in experimental hypothyroidism due to perchlorate can not be prevented with reserpine.

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EFFECT OF ACTINOMYCIN D ON TSH-INDUCED STIMULATION OF THYROIDAL PROTEIN SYNTHESIS IN THE RAT

Acta Endocrinologica ◽

10.1530/acta.0.0770064 ◽

1974 ◽

Vol 77 (1) ◽

pp. 64-70 ◽

Cited By ~ 9

Author(s):

Gustav Wägar

Keyword(s):

Protein Synthesis ◽

Actinomycin D ◽

The Other ◽

Leucine Incorporation ◽

Short Term ◽

Other Hand ◽

Thyroid Glands ◽

Translational Level ◽

Stimulation Of

ABSTRACT Whether the short-term regulation of thyroidal protein synthesis by TSH occurs at the transcriptional or the translational level was tested by measuring the effect of actinomycin D (act D) on the TSH-induced stimulation of L-14C-leucine incorporation into the thyroidal proteins of rats. TSH was injected 6 h before the rats were killed. The thyroid glands were then removed and incubated in vitro in the presence of L-14C-leucine for 2 h. The pronounced stimulation of leucine incorporation in the TSH-treated animals was depressed as compared with controls but still significant even when the animals had been pre-treated with 100 μg act D 24 and 7 h before sacrifice. On the other hand, act D strongly decreased incorporation of 3H-uridine into RNA. Short-term regulation of thyroidal protein synthesis by TSH appears to be partly but not wholly dependent on neosynthesis of RNA. Hence regulation may partly occur at the translation level of protein synthesis.

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