Dual effects of vasoactive intestinal peptide (VIP) on leucocyte migration. 1991

L Bondesson, and K Norolind, and S Lidén, and G Gafvelin, and E Theodorsson, and V Mutt
Department of Dermatology, Karolinska Hospital, Stockholm, Sweden.

Vasoactive intestinal peptide, at different concentrations, was tested on the migration of leucocytes by using the sealed capillary migration test. Vasoactive intestinal peptide, at 10(-7)-10(-9)M, inhibited, while at 10(-12)-10(-14)M, stimulated mononuclear leucocyte migration. The migration of polymorphonuclear leucocytes was inhibited by vasoactive intestinal peptide at 10(-6)-10(-9)M, a stimulation was found at 10(-13)-10(-14)M. The inhibiting effect of vasoactive intestinal peptide on leucocyte migration was abolished when vasoactive intestinal peptide was split into C- and N-terminal fragments, while a stimulating effect was retained in the N-terminal fragment, at 10(-14)M, for mononuclear cells. Helodermin and peptide T, as well as two other members of the secretin-glucagon family, secretin and gastric inhibitory peptide, had no effect on the migration. When VIP antiserum was tested, it had an inhibiting effect, which was not seen with control serum, supporting a physiological effect of the lower vasoactive intestinal peptide concentrations. Vasoactive intestinal peptide seems to have dual effects on mononuclear and polymorphonuclear leucocyte migration and, generally, intact vasoactive intestinal peptide seems to be needed for these effects.

UI MeSH Term Description Entries
D009000 Monocytes Large, phagocytic mononuclear leukocytes produced in the vertebrate BONE MARROW and released into the BLOOD; contain a large, oval or somewhat indented nucleus surrounded by voluminous cytoplasm and numerous organelles. Monocyte
D009504 Neutrophils Granular leukocytes having a nucleus with three to five lobes connected by slender threads of chromatin, and cytoplasm containing fine inconspicuous granules and stainable by neutral dyes. LE Cells,Leukocytes, Polymorphonuclear,Polymorphonuclear Leukocytes,Polymorphonuclear Neutrophils,Neutrophil Band Cells,Band Cell, Neutrophil,Cell, LE,LE Cell,Leukocyte, Polymorphonuclear,Neutrophil,Neutrophil Band Cell,Neutrophil, Polymorphonuclear,Polymorphonuclear Leukocyte,Polymorphonuclear Neutrophil
D010455 Peptides Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are considered to be larger versions of peptides that can form into complex structures such as ENZYMES and RECEPTORS. Peptide,Polypeptide,Polypeptides
D002464 Cell Migration Inhibition Phenomenon of cell-mediated immunity measured by in vitro inhibition of the migration or phagocytosis of antigen-stimulated LEUKOCYTES or MACROPHAGES. Specific CELL MIGRATION ASSAYS have been developed to estimate levels of migration inhibitory factors, immune reactivity against tumor-associated antigens, and immunosuppressive effects of infectious microorganisms. Chemotaxis Inhibition,Chemotaxis Inhibitions,Inhibition, Chemotaxis,Inhibitions, Chemotaxis
D005749 Gastric Inhibitory Polypeptide A gastrointestinal peptide hormone of about 43-amino acids. It is found to be a potent stimulator of INSULIN secretion and a relatively poor inhibitor of GASTRIC ACID secretion. Glucose-Dependent Insulinotropic Peptide,Gastric-Inhibitory Polypeptide,Glucose Dependent Insulinotropic Peptide,Glucose-Dependent Insulin-Releasing Peptide,Glucose Dependent Insulin Releasing Peptide,Inhibitory Polypeptide, Gastric,Insulin-Releasing Peptide, Glucose-Dependent,Insulinotropic Peptide, Glucose-Dependent,Peptide, Glucose-Dependent Insulin-Releasing,Peptide, Glucose-Dependent Insulinotropic,Polypeptide, Gastric Inhibitory,Polypeptide, Gastric-Inhibitory
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D012633 Secretin A peptide hormone of about 27 amino acids from the duodenal mucosa that activates pancreatic secretion and lowers the blood sugar level. (USAN and the USP Dictionary of Drug Names, 1994, p597) Secrepan,Secretin Citrate, Pig,Secretin Maleate, Pig,Secretin Pentacetate, Pig,Secretin Sulfate, Pig,Secretin, Pig,Secretin-KABI,Pig Secretin,Pig Secretin Citrate,Pig Secretin Maleate,Pig Secretin Pentacetate,Pig Secretin Sulfate,Secretin KABI,SecretinKABI
D014660 Vasoactive Intestinal Peptide A highly basic, 28 amino acid neuropeptide released from intestinal mucosa. It has a wide range of biological actions affecting the cardiovascular, gastrointestinal, and respiratory systems and is neuroprotective. It binds special receptors (RECEPTORS, VASOACTIVE INTESTINAL PEPTIDE). VIP (Vasoactive Intestinal Peptide),Vasoactive Intestinal Polypeptide,Vasointestinal Peptide,Intestinal Peptide, Vasoactive,Intestinal Polypeptide, Vasoactive,Peptide, Vasoactive Intestinal,Peptide, Vasointestinal,Polypeptide, Vasoactive Intestinal
D015717 Peptide T N-(N-(N(2)-(N-(N-(N-(N-D-Alanyl L-seryl)-L-threonyl)-L-threonyl) L-threonyl)-L-asparaginyl)-L-tyrosyl) L-threonine. Octapeptide sharing sequence homology with HIV envelope protein gp120. It is potentially useful as antiviral agent in AIDS therapy. The core pentapeptide sequence, TTNYT, consisting of amino acids 4-8 in peptide T, is the HIV envelope sequence required for attachment to the CD4 receptor. HIV Peptide T,Peptide T, HIV
D036341 Intercellular Signaling Peptides and Proteins Regulatory proteins and peptides that are signaling molecules involved in the process of PARACRINE COMMUNICATION. They are generally considered factors that are expressed by one cell and are responded to by receptors on another nearby cell. They are distinguished from HORMONES in that their actions are local rather than distal. Growth Factor,Growth Factors,Paracrine Peptide Factors,Paracrine Protein Factors,Factor, Growth,Factors, Growth,Peptide Factors, Paracrine

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