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
  • 1
    ISSN: 1432-0878
    Keywords: Key words: Collagen ; Matrilysin (PUMP) ; Wound healing ; Tumors ; Fat-storing cells ; Peripheral nerve glial cells ; Fibrocytes ; Human
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. Matrix metalloproteinases represent a family of zinc-dependent proteolytic enzymes thought to be involved in normal and disease-related tissue remodeling processes. Increasing information about these enzymes is becoming available concerning their primary sequences, regulation at the mRNA level, activation of proenzymes, and modulation of enzyme activity by tissue inhibitors. In contrast, their morphological distribution and biological functions in normal tissues are poorly understood. In the present report, the comparative distribution of five members (gelatinase-A, gelatinase-B, matrilysin, stromelysin-1, and stromelysin-3) of the matrix metalloproteinase family and of one inhibitor (TIMP-1) has been morphologically analyzed in human liver and skin with the aid of new monospecific antibodies. Because of their common designation as matrix proteinases, these enzymes might have been expected to be distributed throughout these tissues, or at least in the connective tissue. However, each member of the family produces a highly specific pattern, staining structures such as arteriolar smooth muscle cells, myoepithelial cells in secretory portions or the luminal lining in excretory ducts of dermal sweat glands, liver bile canaliculi, or structures surrounding peripheral nerve axons. No reactivity is detected in rat tissues.
    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
    Langenbeck's archives of surgery 361 (1983), S. 900-900 
    ISSN: 1435-2451
    Keywords: Carcinoma of the colon ; Colonic mucin ; Sialic acid histochemistry ; Lectins ; Coloncarcinom ; Colonmucin ; Sialinsäure-Histochemie ; Lektine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Zusammenfassung In maligne entarteten Geweben sind unvollständig ausgebildete Glykokonjugate häufig. Zur Frühdiagnostik des Coloncarcinoms wurde daher zunächst die Kohlenhydratsequenz des normalen Colonmucins des Menschen untersucht. Mit Sialinsäure- und Lektin-histochemischen Methoden konnte gezeigt werden, daß die terminale O-Acylsialinsäure an das C-6-Atom des vorangehenden N-Acetylgalaktosamins gebunden ist. Daher ist zu vermuten, daß über den Lektin-histochemischen Nachweis Sialinsäure-freier N-Acetylgalaktosaminreste eine Frühdiagnose des Coloncarcinoms möglich ist.
    Notes: Summary Incomplete carbohydrate chains of glycoconjugates commonly occur in malignant tissue. For early diagnosis of carcinoma of the colon, the terminal carbohydrate sequence of normal human colonic mucin was investigated. A combination of sialic acid and lectin histochemical methods showed that the terminal O-acylsialic acids are bound to the carbon-6 of the preceding N-acetylgalactosamine moiety. Therefore, lectin histochemical detection of sialic-acid-free N-acetylgalactosamine residues may be of value for the early diagnosis of cancer of the colon.
    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...