MD PhD Walter Willett - Dairy & Cancer скачать в хорошем качестве

MD PhD Walter Willett - Dairy & Cancer

   • A tale of bugs and foods: Hwp1 versus glut...   MD PhD Walter Willett: https://www.hsph.harvard.edu/walter-w... https://en.wikipedia.org/wiki/Walter_... http://eatforum.org/person/professor-... https://oldwayspt.org/bio/walter-will... DAIRY CONTAINS AT LEAST TWO TRANSGLUTAMINASE SUBSTRATES: CASEIN AND LACTALBUMIN:    • A tale of bugs and foods: Hwp1 versus glut...   Casein is a very good substrate of the transglutaminase catalyzed crosslinking reaction (Simpson 2012). Casein is a known TG2 (tissue transglutaminase) substrate (Forsprecher 2011). Casein is a well-known substrate for factor XIIIa (plasma transglutaminase) (Huff 1999). CASEIN: THE BEST TRANSGLUTAMINASE SUBSTRATE?: http://webs.ono.com/fotgcren/index.htm Casein is a very good substrate of the transglutaminase catalyzed crosslinking reaction (Simpson 2012). Casein is a known TG2 (tissue transglutaminase) substrate (Forsprecher 2011). Casein is a well-known substrate for factor XIIIa (plasma transglutaminase) (Huff 1999). Færgemand and Qvist and Lorenzen and colleagues reported that caseins in general are good substrates for transglutaminase (Monogioudi 2010). The rate of cross-linking by TGase depends on the macromolecular structure of each protein substrate; the open conformation of the casein makes them good substrates (Osullivan 2001). The synthetic pentadecapeptide Ser-Val-Leu-Ser-Leu-Ser-Gln- Ser-Lys-Val-Leu-Pro-Val-Pro-Glu, corresponding in sequence to residues 161 through 175 of Beta-casein has proven to be an excellent substrate for amine incorporation with both human plasma factor XIIIa and guinea pig liver transglutaminase (Gorman 1984). Transglutaminase acyl donor sites in the four individual bovine caseins were determined. Purified caseins labeled with a radioactive site-specific probe in a guinea pig liver transglutaminase-catalyzed reaction were subjected to enzymatic digestion followed by reversed-phase HPLC separation of the resulting peptides. By a combination of sequence and mass spectrometric analysis of the major radioactive fractions, the following TG-reactive glutamine residues were found:  αs1-casein, Gln13, Gln108, Gln130, and Gln140; αs2-casein, Gln79, Gln169, Gln185, and Gln187; β-casein, Gln54, Gln56, Gln72, Gln79, and Gln182; κ-casein, Gln29, Gln45, Gln114, and Gln163. In addition, an intra- or intermolecular cross-link between Gln45 and each of two adjacent lysine residues, Lys21 and Lys24 in monomeric κ-casein, was identified (Christensen 1996). Casein forms abundant oligomers after TG2 incubation (Forsprecher 2011). TRANSGLUTAMINASE AND CANCER Multiple studies have shown elevated TG2 expression in many types of cancer cells, including pancreatic carcinoma, breast carcinoma, malignant melanoma, ovarian carcinoma, lung carcinoma, and glioblastoma (Metha 2010). Many reports have demonstrated down-regulated TG2 expression in primary tumors and upregulated expression in secondary metastatic tumors or those resistant to chemotherapy and its expression has been implicated in disease progression Increased expression of TG2 in cancer cells has been liked to increased drug resistance, metastasis and poor patient survival. These findings suggest an interconnecting link between chronic inflammation, TG2, and progression of metastatic and drug-resistant cancer (Metha 2010). Metastatic tumors from patients with breast cancer, malignant melanoma , and ovarian carcinoma show substantial increases in TG2 expression compared with that in their primary counterparts (Metha 2010).