Library

feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
Filter
  • 1965-1969  (2)
  • Histamine  (1)
  • Permeability
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 261 (1968), S. 252-270 
    ISSN: 1432-1912
    Keywords: Peptides ; Bee Venom ; Mast Cells ; Histamine ; Vascular Permeability ; Peptide ; Bienengift ; Mastzellen ; Histamin ; Gefäßpermeabilität
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Zusammenfassung Bienengift enthält neben dem universell zellschädigenden Melittin und der über Lysolecithinbildung wirksamen Phospholipase A ein drittes mastzelldegranulierendes (MCD-)Peptid. Seine Isolierung gelingt durch Kombination von Gelfiltration an Sephadex G 50 mit Ionenaustauschchromatographie an Carboxymethylcellulose und an Amberlite IRC-50. MCD-Peptid ist stark basisch (Isoelektrischer Punkt um pH 12). Sein minimales Molekulargewicht errechnet sich aus der Aminosäurenanalyse zu 2593. Das Peptid besteht aus 22 Aminosäuren, darunter 4 Halbcystinen. Es liegt in zwei verschiedenen Ladungszuständen vor, die sich bei Papierchromatographie, Papierelektrophorese und Aminosäurenanalyse einheitlich verhalten. MCD-Peptid ist an isolierten Rattenmastzellen (Histaminfreisetzung) und am Mesenterialhäutchen der Ratte (Mastzelldegranulation) etwa wirkungsgleich mit dem synthetischen Histaminliberator Compound 48/80. Melittin wirkt ca. 100- bzw. 10 mal schwächer und zeichnet sich überdies durch eine sehr flache Dosis-Wirkungsbeziehung bei der Histaminfreisetzung aus. Der Rattenblutdruck wird durch MCD-Peptid und Compound 48/80 in quantitativ und qualitativ vergleichbarer Weise gesenkt. Zwischen beiden Substanzen besteht kreuzweise Tachyphylaxie. Die Permeabilität der Hautgefäße der Ratte für zirkulierendes Evans-Blau steigt bei intracutaner Applikation von MCD-Peptid und Compound 48/80. Beide Substanzen sind hier stärker wirksam als Melittin. Die Hautgefäße des Kaninchens sprechen jedoch auf MCD-Peptid schwächer an als auf Melittin und Compound 48/80. Die Ratte reagiert auf i.v. Injektion von 0,5–10 mg/kg MCD-Peptid mit massiver Hyperämie der Acren. Eine kurzdauernde Spastik der Extremitäten weist auf einen zusätzlichen Angriff am motorischen System hin.
    Notes: Summary Bee venom contains three agents which can produce mast cell degranulation. Melittin is a universally acting surfactant; phospholipase A releases the mastocytolytic lysolecithin. A third mast cell degranulating (MCD) peptide has been isolated by gel filtration on Sephadex G 50, followed by chromatography on carboxymethylcellulose, and, finally, on Amberlite IRC-50. MCD-peptide is strongly basic (isoelectric point near pH 12). From the amino acid analysis, a minimum molecular weight of 2593 has been calculated. MCD-peptide consists of 22 amino acids, among them 4 halfcystine residues. It can be obtained in two fractions differing by charge, which appear homogeneous, however, on paper chromatography, paper electrophoresis, and amino acid analysis. When tested on isolated mast cells or on mesentery tissue of rats, MCD-peptide is equiactive with compound 48/80. On the other hand, melittin is 100 times less potent than compound 48/80 on the former tissue and 10 times less potent on the latter; moreover, the dose-response-relation of histamine release is flatter with melittin. MCD-peptide and compound 48/80 depress the blood pressure of rats in a quantitatively and qualitatively similar manner. Crossed tachyphylaxis has been demonstrated. Both substances increase the capillary permeability of rat skin upon intracutaneous injection. Melittin is less active on rat skin vessels. The skin capillaries of rabbits are, however, more sensitive to melittin and compound 48/80 than to MCD-peptide. MCD-peptide (0.5–10 mg/kg i.v.) produces in rats an extreme cyanosis of the acra. A short lasting spasm of the extremities points to an additional effect on the motor system of rats.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 264 (1969), S. 476-493 
    ISSN: 1432-1912
    Keywords: Kinins ; Permeability ; Heat ; Inflammation ; Kinine ; Permeabilität ; Hitze ; Entzündung
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary 1. The suboutis of rat paws heated (46,5° C) in situ has been perfused. Kinin activity could be demonstrated regularly in the fluid which was collected in ice. When the solutions were tested immediately after having passed the tissue, only some of the experiments yielded positive results. Native and125Jlabelled kininogen as well as kininogenase and kininase activities passed into the perfusates. The sensitivity to dextran and the kinin release on heating were, in contrast to recent reports, not correlated. 2. The release of the components of the kinin system approximately paralleled that of labelled human albumin. Their concentration rose until about 1 hour after the start of the heating. There was no priority of the components of the kinin system when compared with human albumin which can be regarded as permeability indicator. 3. Intravenously injected carboxypeptidase B, because of its lower molecular weight, entered the interstitial fluid more easily than did the plasma carboxypeptidase N. Its blood level decreased rapidly; but sufficient tissue concentrations could be maintained by intravenous infusions. Neither the volume nor the time dependence of the thermic edema changed during carboxypeptidase B-infusions. The same was true for infusions of trasylol, whereas phenylbutazone inhibited the edema significantly. Edema formed by short heating (30 sec, 55° C) was equally resistant to carboxypeptidase B. 4. In the skin and muscles of the heated rat paw, carbon particles mainly stained the capillary walls. This finding argues against a considerable involvement of “classical” mediators which should induce venular lesions. 5. Infusion of large amounts of bradykinin into the arterial supply did not imitate the thermic edema; neither has bradykinin been found in the perfusate of the subcutis. 6. In the light of these findings, a significant role of the kinin system in the thermic edema of the rat paw is to be doubted.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...