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1.
Semin Cancer Biol ; 60: 324-333, 2020 02.
Article in English | MEDLINE | ID: mdl-31647982

ABSTRACT

The macro-metastasis/organ parenchyma interface (MMPI) was previously considered an inert anatomical border which sharply separates the affected organ parenchyma from the macro-metastatic tissue. Recently, infiltrative growth of macro-metastases from various primary tumors was described in the brain, liver and lung, with significant impact on survival. Strikingly, the MMPI patterns differed between entities, so that at least nine different patterns were described. The MMPI patterns could be further classified into three major groups: displacing, epithelial and diffuse infiltrating. Additionally, macro-metastases are a source of further tumor cell dissemination in the affected organ; and these intra-organ metastatic dissemination tracks starting from the MMPI also vary depending on the anatomical structures of the colonized organ and influence disease outcome. In spite of their relevance, MMPIs and organ-specific dissemination tracks are still largely overlooked by many clinicians, pathologists and/or researchers. In this review, we aim to address this important issue and enhance our current understanding of the different MMPI patterns and dissemination tracks in the brain, liver and lung.


Subject(s)
Neoplasms/diagnosis , Humans , Neoplasm Invasiveness , Neoplasm Metastasis , Neoplasm Staging , Neoplasms/etiology , Neoplasms/metabolism , Organ Specificity
2.
Z Lebensm Unters Forsch ; 157(4): 197-204, 1975 Apr 07.
Article in German | MEDLINE | ID: mdl-1229711

ABSTRACT

Two bitter peptides, H-Phe-Tyr-Pro-Glu-Leu-Phe-OH (I) and H-Val-Glu-Val-Phe-Ala-Pro-Pro-Phe-OH (II) were isolated from casein, hydrolyzed by alpha-chymotrypsin. The hexapeptide is cleaved by thermolysine between Glu and Leu. The two fragments are bitter too. A bitter dodecapeptide (III) was obtained 20 min hydrolysis of casein with trypsin. On account of amino acid composition and N-terminus peptide III is probably identical with a peptide from a 12 hrs hydrolyzate, described in 1970 by Matoba. The peptides I and III have equal taste tresholds in the range of 0.08-0.10 muM/ml.


Subject(s)
Caseins/analysis , Peptides/isolation & purification , Chymotrypsin , Hydrolysis , Methods , Taste , Trypsin
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