Actin binding to lipid-inserted alpha-actinin

Fritz, Monika; Zimmermann, R.; Bärmann, M.; Gaub, Hermann E.

doi:10.1016/s0006-3495(93)81252-9

Cited by 22 publications

(15 citation statements)

References 57 publications

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“…In addition, the I band shrunk (0.13 μm) and the A band was enlarged (1.57 μm) compared with live fish muscle ( P < 0.05), which indicated that the cytoskeletal connections between the myofibrils had been altered already (Papa and others ). According to previous studies, the damage of I bands and the segmentation of myofibrils resulted from the delocalization of α‐actinin (Fritz and others , Saad ). Compared with live muscle, there existed a clear Z line but a fainter M line and a thinner I band (0.27 μm) for fillets at –3 °C (Figure (C)), which underwent less change than fillets at 4 °C.…”

Section: Resultsmentioning

confidence: 87%

Effects of Chilling and Partial Freezing on Rigor Mortis Changes of Bighead Carp (Aristichthys nobilis) Fillets: Cathepsin Activity, Protein Degradation and Microstructure of Myofibrils

Han

Liu

Zhang

et al. 2015

Journal of Food Science

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To investigate the effects of chilling and partial freezing on rigor mortis changes in bighead carp (Aristichthys nobilis), pH, cathepsin B, cathepsin B+L activities, SDS-PAGE of sarcoplasmic and myofibrillar proteins, texture, and changes in microstructure of fillets at 4 °C and -3 °C were determined at 0, 2, 4, 8, 12, 24, 48, and 72 h after slaughter. The results indicated that pH of fillets (6.50 to 6.80) was appropriate for cathepsin function during the rigor mortis. For fillets that were chilled and partially frozen, the cathepsin activity in lysosome increased consistently during the first 12 h, followed by a decrease from the 12 to 24 h, which paralleled an increase in activity in heavy mitochondria, myofibrils and sarcoplasm. There was no significant difference in cathepsin activity in lysosomes between fillets at 4 °C and -3 °C (P > 0.05). Partially frozen fillets had greater cathepsin activity in heavy mitochondria than chilled samples from the 48 to 72 h. In addition, partially frozen fillets showed higher cathepsin activity in sarcoplasm and lower cathepsin activity in myofibrils compared with chilled fillets. Correspondingly, we observed degradation of α-actinin (105 kDa) by cathepsin L in chilled fillets and degradation of creatine kinase (41 kDa) by cathepsin B in partially frozen fillets during the rigor mortis. The decline of hardness for both fillets might be attributed to the accumulation of cathepsin in myofibrils from the 8 to 24 h. The lower cathepsin activity in myofibrils for fillets that were partially frozen might induce a more intact cytoskeletal structure than fillets that were chilled.

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Section: Resultsmentioning

confidence: 87%

Effects of Chilling and Partial Freezing on Rigor Mortis Changes of Bighead Carp (Aristichthys nobilis) Fillets: Cathepsin Activity, Protein Degradation and Microstructure of Myofibrils

Han

Liu

Zhang

et al. 2015

Journal of Food Science

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“…In contrast to the MLVs containing negatively charged DMPG, none of the charge isomers had a significant effect on the absorbance of neutral DMPC MLVs at 23°C (Table I). Because the inclusion of diacylglycerol has been reported to increase the interaction of some proteins with lipid despite its lack of charged groups (Soulages et al, 1995;Arnold et al, 1997;Fritz et al, 1993), the effect of MBP isomers on MLVs of DMPC/DAG 95:5 (m/m) and DMPC/DMPG/DAG (75: 20:5) was determined. The inclusion of DAG in either neutral DMPC or negatively charged DMPC/DMPG MLVs had no significant effect on the aggregation caused by any of the charge isomers (Table I).…”

Section: Resultsmentioning

confidence: 99%

Highly deiminated isoform of myelin basic protein from multiple sclerosis brain causes fragmentation of lipid vesicles

et al. 1999

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Myelin basic protein (MBP) occurs as a number of charge isomers due to phosphorylation, deamidation, and deimination of arginine to citrulline. All of these modifications decrease the net positive charge of the protein and its ability to cause aggregation of negatively charged lipid vesicles. This is used as a model system for the ability of MBP to cause adhesion of the cytosolic surfaces of myelin. Therefore, the effect of two deiminated forms of MBP on lipid vesicles was compared with that of the unmodified, most positively charged isomer, C1, to determine how loss of positively charged arginines would affect the function of MBP. The deiminated forms were the isomer isolated from normal human brains, in which only 6 Arg are deiminated to citrulline (MBP-Cit(6)), and an isomer isolated from the brain of a patient who died with acute, fulminating multiple sclerosis (Marburg type), in which 18 of the 19 Arg were deiminated (MBP-Cit(18)). Whereas C1 caused aggregation of lipid vesicles, resulting in an increase in absorbance due to light scattering, MBP-Cit(18) caused a decrease in absorbance of the lipid vesicles. Size exclusion chromatography and negative staining electron microscopy showed that this was due to fragmentation of the large multilayered vesicles into much smaller vesicles. MBP-Cit(6) caused less aggregation of lipid vesicles than did C1. However, no fragmentation of the vesicles into smaller ones in the presence of C1 and MBP-Cit(6) was detected by size exclusion chromatography or electron microscopy. The membrane fragmentation caused by MBP-Cit(18) is dramatically different from the effects of other forms of MBP from normal brain and may indicate a pathogenic effect of this charge isomer, which may have contributed to the severity of the Marburg type of multiple sclerosis. Alternatively, the deimination may have been a secondary effect resulting from the disease process. Regardless of the role of MBP-Cit(18) in multiple sclerosis, the effect of this modification indicates that, when most of the arginines of MBP are modified to an uncharged amino acid, the protein acquires properties similar to an apolipoprotein; thus, it may take up an amphipathic structure when bound to lipid. A partly amphipathic character may also be related to the role of MBP-Cit(6) in normal immature myelin, where it is the predominant charge isomer.

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“…Typical examples are biomolecular recognition (1), cytoskeleton-membrane coupling (2,3), and interfacial activity of membrane-associated enzymes such as phospholipases (4)(5)(6).…”

Section: Introductionmentioning

confidence: 99%

Development of a Constant Surface Pressure Penetration Langmuir Balance Based on Axisymmetric Drop Shape Analysis

Wege

Holgado-Terriza

Cabrerizo-Vílchez

2002

Journal of Colloid and Interface Science

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Actin binding to lipid-inserted alpha-actinin

Cited by 22 publications

References 57 publications

Effects of Chilling and Partial Freezing on Rigor Mortis Changes of Bighead Carp (Aristichthys nobilis) Fillets: Cathepsin Activity, Protein Degradation and Microstructure of Myofibrils

Effects of Chilling and Partial Freezing on Rigor Mortis Changes of Bighead Carp (Aristichthys nobilis) Fillets: Cathepsin Activity, Protein Degradation and Microstructure of Myofibrils

Highly deiminated isoform of myelin basic protein from multiple sclerosis brain causes fragmentation of lipid vesicles

Development of a Constant Surface Pressure Penetration Langmuir Balance Based on Axisymmetric Drop Shape Analysis

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