Binding of Soluble Myelin Basic Protein to Various Conformational Forms of α2-Macroglobulin

Gunnarsson, Martin; Jensen, Poul Erik

doi:10.1006/abbi.1998.0902

Cited by 14 publications

(6 citation statements)

References 44 publications

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“…We note several other published protein associations of MBP, including Limulus hemocyanin (Groschel-Stewart et al, 1997), a 2 -macroglobulin (Gunnarsson and Jensen, 1998;Gunnarsson et al, 2003), and the constitutive heat shock protein 70 (Aquino et al, 1998;Cwiklinska et al, 2003). The first of these interactions is unusual, but the latter two appear also to be involved in MS and, thus, be of physiological relevance.…”

Section: Mbp Binds Other Myelin and Non-myelin Proteinsmentioning

confidence: 83%

Myelin basic protein—diverse conformational states of an intrinsically unstructured protein and its roles in myelin assembly and multiple sclerosis

Harauz

Ishiyama

Hill

et al. 2004

Micron

233

209

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Section: Mbp Binds Other Myelin and Non-myelin Proteinsmentioning

confidence: 83%

Myelin basic protein—diverse conformational states of an intrinsically unstructured protein and its roles in myelin assembly and multiple sclerosis

Harauz

Ishiyama

Hill

et al. 2004

Micron

233

209

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“…The release of myelin basic protein after serious trauma results in an immunogenic material that can lead to immunoreactive demyelination. Binding of myelin by a 2 M is now believed to blunt the immunological response to myelin basic protein (30).…”

Section: Introductionmentioning

confidence: 99%

Reference distributions for alpha₂‐macroglobulin: A practical, simple and clinically relevant approach in a large cohort

Ritchie

Palomaki

Neveux

et al. 2004

Clinical Laboratory Analysis

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In this 11th article in a series, reference values of serum levels alpha(2)-macroglobulin alpha(2)M) are examined. The study is based on a cohort of 40,420 Caucasian individuals from northern New England that were tested in our laboratory between 1994 and 2000. Measurements were standardized against Certified Reference Material (CRM 470)/Reference Preparation for Proteins in Human Serum (RPPHS) and the results analyzed using a previously described statistical approach. Individuals with unequivocal laboratory evidence of inflammation (C-reactive protein >10 mg/L) were excluded in one leg of the study and included in the other, confirming that alpha(2)M does not respond to acute phase drive in man. Nephrotic syndrome, diabetes mellitus, and chronic liver disease have significant effect on levels of alpha(2)M. Dramatic changes occur during life with males higher from birth to age 12, females thereafter have higher values until the ninth decade. When values were expressed as multiples of the age- and gender-specific median levels, the resulting distributions fitted a log-Gaussian distribution well over a broad range. When patient data are normalized in this manner, the distribution parameters can be used to assign a centile corresponding to an individual's measurement thus simplifying interpretation.

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“…In addition to proteinases, ␣ 2 M binds a variety of functionally dissimilar proteins, including cytokines and growth factors, ␤-amyloid peptide, apolipoprotein E, myelin basic protein, and leptin (15)(16)(17)(18)(19)(20). Although it is possible that some of these interactions depend on intact ␣ 2 M quaternary structure, we recently identified a linear sequence in ␣ 2 M that serves as a binding site for transforming growth factor-␤1 (TGF-␤1) and TGF-␤2 (21).…”

mentioning

confidence: 99%

Identical or Overlapping Sequences in the Primary Structure of Human α2-Macroglobulin Are Responsible for the Binding of Nerve Growth Factor-β, Platelet-derived Growth Factor-BB, and Transforming Growth Factor-β

Gonias¹,

Carmichael²,

Mettenburg³

et al. 2000

Journal of Biological Chemistry

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Binding of Soluble Myelin Basic Protein to Various Conformational Forms of α2-Macroglobulin

Cited by 14 publications

References 44 publications

Myelin basic protein—diverse conformational states of an intrinsically unstructured protein and its roles in myelin assembly and multiple sclerosis

Myelin basic protein—diverse conformational states of an intrinsically unstructured protein and its roles in myelin assembly and multiple sclerosis

Reference distributions for alpha₂‐macroglobulin: A practical, simple and clinically relevant approach in a large cohort

Identical or Overlapping Sequences in the Primary Structure of Human α2-Macroglobulin Are Responsible for the Binding of Nerve Growth Factor-β, Platelet-derived Growth Factor-BB, and Transforming Growth Factor-β

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Binding of Soluble Myelin Basic Protein to Various Conformational Forms of α2-Macroglobulin

Cited by 14 publications

References 44 publications

Myelin basic protein—diverse conformational states of an intrinsically unstructured protein and its roles in myelin assembly and multiple sclerosis

Myelin basic protein—diverse conformational states of an intrinsically unstructured protein and its roles in myelin assembly and multiple sclerosis

Reference distributions for alpha2‐macroglobulin: A practical, simple and clinically relevant approach in a large cohort

Identical or Overlapping Sequences in the Primary Structure of Human α2-Macroglobulin Are Responsible for the Binding of Nerve Growth Factor-β, Platelet-derived Growth Factor-BB, and Transforming Growth Factor-β

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Product

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About

Reference distributions for alpha₂‐macroglobulin: A practical, simple and clinically relevant approach in a large cohort