Influence of Diet and Stage of Lactation on Taurine Contents in Milk

Blomberg, Bme von; Trautwein, Elke A.; Erbersdobler, Helmut F.

doi:10.1007/978-3-642-85373-9_48

Cited by 1 publication

(1 citation statement)

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“…It is worth noting that taurine alone can decrease the heat-induced aggregation of catalase by 22% (Table 1).Therefore, it might be possible that taurine alters α-casein chaperone activity and at the same time inhibits heat-induced aggregation of catalase. Both α-casein and taurine have been found to co-exist in the mammalian breast milk, with taurine concentration ranging from 100-700 μM 42,43 . However, during stress and disease conditions, concentration of osmolytes may go up to millimolar range 29,37 .…”

Section: Discussionmentioning

confidence: 99%

Taurine Induces an Ordered but Functionally Inactive Conformation in Intrinsically Disordered Casein Proteins

Bhat

Singh

Dar

2020

Sci Rep

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intrinsically disordered proteins (iDps) are involved in various important biological processes, such as cell signalling, transcription, translation, cell division regulation etc. Many iDps need to maintain their disordered conformation for proper function. osmolytes, natural organic compounds responsible for maintaining osmoregulation, have been believed to regulate the functional activity of macromolecules including globular proteins and iDps due to their ability of modulating the macromolecular structure, conformational stability, and functional integrity. in the present study, we have investigated the effect of all classes of osmolytes on two model IDPs, αand β-casein. it was observed that osmolytes can serve either as folding inducers or folding evaders. folding evaders, in general, do not induce iDp folding and therefore had no significant effect on structural and functional integrity of IDPs. On the other hand, osmolytes taurine and tMAo serve as folding inducers by promoting structural collapse of iDps that eventually leads to altered structural and functional integrity of iDps. this study sheds light on the osmolyte-induced regulation of iDps and their possible role in various disease pathologies. A well-defined, stable three dimensional structure was once thought to be an essential prerequisite for proper function of a protein 1-3. However, during the last few decades biologically active proteins without well-defined stable tertiary structures have also been found in most of the proteomes 4-6. These proteins are often referred as intrinsically disordered proteins (IDPs) or natively unfolded proteins 7-10. One of the distinctive feature of IDPs is the presence of relatively low number of hydrophobic and aromatic amino acid residues and high number of charged and polar residues 11-15. The absence of stable structure allows these proteins to exist as highly dynamic conformational ensembles containing a wide variety of rapidly interconverting structures, thereby providing means for interaction with multiple often unrelated partners and for performing various important physiological functions 12,15-19. These proteins once known as a small group of rare exceptions are being presently explored for their central roles in the regulation of various key cellular processes including signal transduction and molecular recognition, mRNA metabolism, translation, transcription, and cell cycle 8,10,15,18,20,21. Additionally, many of such IDPs function as chaperones in different tissues 22. More importantly, numerous IDPs have been found to be associated with the pathophysiology of various human diseases including diabetes, amyloidosis, neurodegeneration, cancer and cardiovascular diseases etc 9,19,23-25. The general mechanisms for the functional regulation of IDPs have been enigmatic. It has been known that the degree of disorderness is one signifying feature for the appropriate functioning of the IDPs 9,17,21,26,27. A flexible structural organization helps various IDPs to interact with multiple binding partners so as to...

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