What is the clinical evidence from this study?

Study design: Other. Intervention: Site-directed mutagenesis of TPO. Primary outcome: Specific bioactivity of TPO protein.

January 1, 1998Journal of Biological ChemistryOpen Access

Identification of Functionally Important Residues of Human Thrombopoietin

View Full Paper

Ask AI

Bookmark

Key result

Alanine substitutions at Arg10, Pro42, Glu50, and Lys138 nearly or completely abolished TPO bioactivity, suggesting these residues are functionally important in interacting with its receptor.

Population

COS7 cells for transient expression of TPO muteins and a recombinant BaF3 cell line expressing human c-Mpl…

Comparison

Site-directed mutagenesis of human… vs Wild-type TPO and other TPO mutants

Design

Preclinical

Authors

HPHeungrok Park SPSung Sup ParkMayo Clinic JSJin-Soo Song

Discussion

Member takes

Implication

Key TPO residues may guide mimetic design; leaves open human translation from animal data.

Structured PICO

Population

COS7 cells for transient expression of TPO muteins and a recombinant BaF3 cell line expressing human c-Mpl for bioactivity measurement

Intervention

Site-directed mutagenesis of human thrombopoietin (TPO) using nonnative N-linked glycosylation scan of 12 residues and alanine replacement scan of 44 residues

Comparator

Wild-type TPO and other TPO mutants

Outcome

Specific bioactivity of the TPO protein secreted into the culture mediumsurrogate

Identification of specific amino acid residues in human thrombopoietin essential for receptor binding provides structural insights into its mechanism of action.

Cite This Study

Park et al. (1998) studied this question. Site-directed mutagenesis of TPO was evaluated on Specific bioactivity of TPO protein. Alanine substitutions at Arg10, Pro42, Glu50, and Lys138 nearly or completely abolished TPO bioactivity, suggesting these residues are functionally important in interacting with its receptor.

synapsesocial.com/papers/6a9b8dd2c12994f0dcbb0078 https://doi.org/10.1074/jbc.273.1.256

View Full Paper

Ask AI

Bookmark

January 1, 1998Journal of Biological ChemistryOpen Access

Identification of Functionally Important Residues of Human Thrombopoietin

View Full Paper

Ask AI

Bookmark

Key result

Alanine substitutions at Arg10, Pro42, Glu50, and Lys138 nearly or completely abolished TPO bioactivity, suggesting these residues are functionally important in interacting with its receptor.

Population

COS7 cells for transient expression of TPO muteins and a recombinant BaF3 cell line expressing human c-Mpl…

Comparison

Site-directed mutagenesis of human… vs Wild-type TPO and other TPO mutants

Design

Preclinical

Authors

HPHeungrok Park SPSung Sup ParkMayo Clinic JSJin-Soo Song

Discussion

Member takes

Implication

Key TPO residues may guide mimetic design; leaves open human translation from animal data.

Structured PICO

Population

COS7 cells for transient expression of TPO muteins and a recombinant BaF3 cell line expressing human c-Mpl for bioactivity measurement

Intervention

Site-directed mutagenesis of human thrombopoietin (TPO) using nonnative N-linked glycosylation scan of 12 residues and alanine replacement scan of 44 residues

Comparator

Wild-type TPO and other TPO mutants

Outcome

Specific bioactivity of the TPO protein secreted into the culture mediumsurrogate

Identification of specific amino acid residues in human thrombopoietin essential for receptor binding provides structural insights into its mechanism of action.

Cite This Study

synapsesocial.com/papers/6a9b8dd2c12994f0dcbb0078 https://doi.org/10.1074/jbc.273.1.256

Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

View Full Paper

Ask AI

Bookmark