Maria C. Linder

ORCID: 0000-0003-3937-9268
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About
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Research Areas
  • Trace Elements in Health
  • Iron Metabolism and Disorders
  • Heavy Metal Exposure and Toxicity
  • Drug Transport and Resistance Mechanisms
  • Hemoglobinopathies and Related Disorders
  • Orthopaedic implants and arthroplasty
  • RNA regulation and disease
  • RNA modifications and cancer
  • Plant Micronutrient Interactions and Effects
  • RNA and protein synthesis mechanisms
  • Molecular Biology Techniques and Applications
  • Aluminum toxicity and tolerance in plants and animals
  • Diet and metabolism studies
  • Enzyme Structure and Function
  • Calcium signaling and nucleotide metabolism
  • Pharmacological Effects of Medicinal Plants
  • Corrosion Behavior and Inhibition
  • Hereditary Neurological Disorders
  • Protein Hydrolysis and Bioactive Peptides
  • Erythrocyte Function and Pathophysiology
  • Vitamin K Research Studies
  • Metabolism and Genetic Disorders
  • Extraction and Separation Processes
  • Agricultural and Biological Research
  • Muscle metabolism and nutrition

California State University, Fullerton
2012-2022

California State University System
1991-2017

Fullerton College
2017

École Normale Supérieure - PSL
2005

Washington University in St. Louis
1990-1994

The University of Texas Medical Branch at Galveston
1986

Linde (United States)
1986

Massachusetts Institute of Technology
1971-1983

Naval Submarine Medical Research Laboratory
1983

Deaconess Hospital
1964

Mechanisms of guanosine triphosphate (GTP) hydrolysis by members the G protein alpha subunit-p21ras superfamily triphosphatases have been studied extensively but not well understood. High-resolution x-ray structures GTP gamma S and GDP.AlF4- complexes formed Gi 1 demonstrate specific roles in transition-state stabilization for two highly conserved residues. Glutamine204 (Gln61 p21ras) stabilizes orients hydrolytic water trigonal-bipyramidal transition state. Arginine 178 negative charge at...

10.1126/science.8073283 article EN Science 1994-09-02

How ferritin-Fe becomes available for cell functions is unknown. Our previous studies with rat hepatoma cells indicated ferritin had to be degraded release its Fe. In these studies, we investigated whether this occurs in other types and lysosomes are required. Release of was induced desferoxamine (DFO) 59 Fe-preloaded hepatoma, Caco2, erythroid K562 measured by rocket immunoelectrophoresis autoradiography. The half-lives ferritin- Fe protein were parallel (23, 16, 11 h the hepatic, cells,...

10.1152/ajpcell.00505.2005 article EN AJP Cell Physiology 2006-04-13

Ceruloplasmin, the main copper binding protein in blood plasma, has been of particular interest for its role efflux iron from cells, but additional functions. Here we tested hypothesis that it releases cell uptake by interacting with a surface reductase and transporters, producing apoceruloplasmin. Uptake transepithelial transport ceruloplasmin was demonstrated mammary epithelial monolayers (PMC42) tight junctions grown bicameral chambers, purified human 64Cu-labeled secreted HepG2 cells....

10.1371/journal.pone.0149516 article EN cc-by PLoS ONE 2016-03-02

The time course of distribution high-specific activity 67CuCl2 to tissues and plasma components was followed in adult, female rats. Immediately after intubation or injection, tracer 67Cu associated with two the blood separable on columns Sephadex G-150: albumin another (larger) component, which not ceruloplasmin. latter, tentatively named transcuprein, had an apparent molecular weight 270,000 a high affinity for Cu2+, as judged by processing through Chelex-100, dilution, exchange copper,...

10.1152/ajpendo.1985.249.1.e77 article EN AJP Endocrinology and Metabolism 1985-07-01

Ionic copper entering blood plasma binds tightly to albumin and the macroglobulin transcuprein. It then goes primarily liver kidney except in lactation, where a large portion directly mammary gland. Little is known about how this taken up from these proteins. To examine this, kinetics of uptake purified human alpha(2)-macroglobulin, effects inhibitors, were measured using hepatic (HepG2) epithelial (PMC42) cell lines. At physiological concentrations (3-6 muM), both types took proteins...

10.1152/ajpcell.00029.2008 article EN AJP Cell Physiology 2008-06-26

10.1016/0003-2697(72)90189-3 article EN Analytical Biochemistry 1972-07-01

We examined the distribution of copper among four components human serum separated by chromatography on Sephadex G-150 and Affi-gel blue. Analysis furnace atomic absorption indicated that normal adults have at an average 600 ng/ml associated with ceruloplasmin; 120 transcuprein, a new transport protein; 150 albumin; 90 one to three low molecular weight (less than 30,000). Cancer patients had more total but similar proportions in fractions. In both groups, some individuals very high levels...

10.1093/jnci/75.2.277 article EN JNCI Journal of the National Cancer Institute 1985-08-01

10.1016/0020-711x(86)90055-8 article EN International Journal of Biochemistry 1986-01-01

Ceruloplasmin was assayed as enzyme activity, antigen, and total copper in serum samples from 150 male lung cancer patients comparable numbers of controls. By all three assays, ceruloplasmin significantly increased above the normal before treatment, degree elevation related to TNM stage [i.e., International Union Against Cancer classification system based on extent primary tumor (T), condition lymph nodes (N), absence presence metastases (M)]. Surgery had no immediate effects, but who...

10.1093/jnci/67.2.263 article EN JNCI Journal of the National Cancer Institute 1981-08-01

In copper-deficient rats, oral intubation of copper increases the rate ceruloplasmin synthesis without affecting general plasma or liver proteins. It also restores enzyme from half to full activity. Copper given by injection at doses commonly employed has additional nonspecific effects on protein and in some strains rats produces severe hemolysis. contrast deficient normal does not elevate unless hemolysis occurs. Thus, least deficiency, availability controls synthesis, activation,...

10.1159/000458625 article EN Enzyme 1979-01-01

10.1016/0304-4165(77)90064-2 article EN Biochimica et Biophysica Acta (BBA) - General Subjects 1977-10-01
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