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C. Benson Kuo, PhD - USC School of Pharmacy. Los Angeles, CA, US

C. Benson Kuo, PhD C. Benson Kuo, PhD

Assistant Professor | USC School of Pharmacy

Los Angeles, CA, UNITED STATES

C. Benson Kuo's research focuses on regulatory issues for innovative medical products and product safety in Asia.

Biography

Dr. C. Benson Kuo is the Associate Director of the Consulting Center. He acts as consultant for regulatory compliance, submission requirements, and strategic planning for innovative products developed at USC or by community members. Prior to joining the program, he served as the regulatory affairs manager at Alfred E. Mann Institute, responsible for regulatory support of medical device development and regulatory submissions and compliance with the FDA and IRBs.

Before embarking on his regulatory affairs career, he worked in biotech industry and served as bioinformatics scientist, patent scientist and patent agent.

Dr. Kuo completed his Ph.D. in the field of biomedical sciences and received postdoctoral training at the Stanford University School of Medicine. He is a graduate of the Regulatory Science program and RAC-certified by the Regulatory Affairs Professional Society (RAPS). He is a member of RAPS, OCRA (Orange County Regulatory Affairs Discussion Group), and the CSTA RK group (Clinical and Translational Science Award Regulatory Knowledge).

Areas of Expertise (6)

Regulatory Strategies

Regulatory Intelligence

Regulatory Submissions

Regulatory Audits

Patent Term Extensions

Asian Regulatory Environment

Education (4)

Stanford University: Postdoctoral Fellow

UC Riverside: Ph.D., Biomedical Sciences

University of Southern California: M.S.

Tunghai University: B.S.

Affiliations (3)

  • OCRA (Orange County Regulatory Affairs Discussion Group) : Member
  • CSTA RK group (Clinical and Translational Science Award Regulatory Knowledge) : Member
  • Regulatory Affairs Professional Society (RAPS) : Member

Patents (3)

Methods and materials relating to cd84-like polypeptides and polynucleotides

US20110268724A1

2011 The invention provides novel polynucleotides and polypeptides encoded by such polynucleotides and mutants or variants thereof that correspond to a novel human secreted CD84-like polypeptide. These polynucleotides comprise nucleic acid sequences isolated from cDNA library from human spleen (Hyseq clone identification numbers 2938352 (SEQ ID NO: 1)). Other aspects of the invention include vectors containing processes for producing novel human secreted CD84-like polypeptides, and antibodies specific for such polypeptides.

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Methods and compositions concerning antibodies that bind CD84-like polypeptides

US7981413B2

2011 The invention provides novel polynucleotides and polypeptides encoded by such polynucleotides and mutants or variants thereof that correspond to a novel human secreted CD84-like polypeptide. These polynucleotides comprise nucleic acid sequences isolated from cDNA library from human spleen (Hyseq clone identification numbers 2938352 (SEQ ID NO: 1)). Other aspects of the invention include vectors containing processes for producing novel human secreted CD84-like polypeptides, and antibodies specific for such polypeptides.

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Methods and Materials Relating to CD84-like Polypeptides and Polynucleotides

US20090042199A1

2009 The invention provides novel polynucleotides and polypeptides encoded by such polynucleotides and mutants or variants thereof that correspond to a novel human secreted CD84-like polypeptide. These polynucleotides comprise nucleic acid sequences isolated from cDNA library from human spleen (Hyseq clone identification numbers 2938352 (SEQ ID NO: 1)). Other aspects of the invention include vectors containing processes for producing novel human secreted CD84-like polypeptides, and antibodies specific for such polypeptides.

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Selected Articles (3)

Effects of prolactin on osteoblast alkaline phosphatase and bone formation in the developing rat American Journal of Physiology-Endocrinology And MetabolismF

Djurdjica Coss, Lili Yang, Chiaoyun Benson Kuo, Xiaolei Xu, Richard A. Luben, and Ameae M. Walker

2000 The purpose of the current study was to determine whether maternal prolactin (PRL) had any effects on bone formation in the developing rat pup. Because the most prevalent forms of PRL in rats are unmodified and phosphorylated PRL, both recombinant PRL and a molecular mimic of phosphorylated PRL (PP-PRL) were administered to pregnant animals. Blood samples from the dams showed normal estrogen and progesterone and no effect of extra PRL on parathyroid hormone (PTH), calcium, or alkaline phosphatase (AP). In newborn pups, however, there was a 30% decrease in blood AP in both PRL-treated groups, whereas PTH and calcium levels were not different from controls. When primary rat osteoblasts were exposed to both PRLs, AP activity was reduced, with PP-PRL being the more potent form of the hormone. Histological examination of pup bone formation showed reduced calvarial bone and reduced endochondral ossification in pups exposed to PP-PRL. These results are the first to show a direct inhibitory effect of PRL on osteoblast function.

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Dissociation of Janus Kinase 2 and Signal Transducer and Activator of Transcription 5 Activation after Treatment of Nb2 Cells with a Molecular Mimic of Phosphorylated Prolactin EndocrinologyF

Djurdjica Coss, Chiaoyun Benson Kuo, Lili Yang, Patricia Ingleton, Richard Luben, Ameae M. Walker

1999 We have previously demonstrated that phosphorylated PRL acts as an antagonist to the Nb2 proliferative activities of unmodified PRL. A molecular mimic of phosphorylated PRL, which substitutes an aspartate residue for the normally phosphorylated serine (serine 179), has the same properties. Because it takes less than one fourth the amount of phosphorylated hormone, or the aspartate mutant, to block the proliferative activity of unmodified hormone, we have investigated whether the high potency of the aspartate mutant is achieved by the production of an alternate and interfering intracellular signal cascade. Nb2 cells were exposed to 5 or 500 ng/ml human NIDDK PRL, wild-type recombinant PRL (unmodified PRL), or aspartate mutant PRL (pseudophosphorylated PRL) for 1, 5, or 10 min at 37 C. At 5 ng/ml and 10 min, wild-type recombinant PRL showed greater activation of Janus kinase 2 (JAK 2) than the NIDDK preparation. This is consistent with a previous report of higher proliferative activity for the wild-type hormone and is primarily a reflection of the presence of some phosphorylated hormone in the NIDDK preparation. At 500 ng/ml and 10 min, saturation eliminated any differences between responses to the two preparations. JAK 2 activation was not seen in response to the aspartate mutant at either concentration. Signal transducer and activator of transcription 5 (STAT 5) activation was, however, just as robust for the aspartate-treated cells as for the other two groups. Time course experiments eliminated the possibility that STAT 5 phosphorylation in response to the aspartate mutant was the result of JAK 2 activation at earlier time points. Experiments in the present study also interestingly showed preassociation of JAK 2 and STAT 5 in the absence of PRL and the absence of detectable phosphorylation of either JAK 2 or STAT 5. Like JAK 2, receptor phosphorylation was absent with the aspartate mutant. A comparison between STAT 5a and STAT 5b activation showed a marked reduction in STAT 5b phosphorylation in response to the aspartate mutant, with concomitant reduction in STAT 5a-STAT 5b heterodimers. STAT 5a activation, however, was indistinguishable between the wild-type and aspartate mutant. We conclude that the nonproliferative aspartate mutant signals and activates STAT 5 without, or with minimal, use of JAK 2 or receptor phosphorylation. The wild-type proliferative PRL, on the other hand, uses receptor phosphorylation and JAK 2 activation.

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Development of Recombinant Human Prolactin Receptor Antagonists by Molecular Mimicry of the Phosphorylated Hormone EndrocrinologyF

Tian-Jian Chen, Chiaoyun Benson Kuo, Kolistin F. Tsai, Jo-Wen Liu, Dih-Yih Chen, Ameae M. Walker

1998 Previous studies have demonstrated that naturally phosphorylated PRL antagonizes the growth-promoting effects of unmodified PRL in two different PRL-responsive cell lines. In this study our aim was to produce a molecular mimic of phosphorylated PRL by substituting a fairly bulky, negatively charged amino acid (glutamate or aspartate) for the normally phosphorylated serine [serine 179 in human PRL (hPRL)]. In addition, because of the marked effect of phosphorylation on biological activity, we investigated the importance of the unmodified serine in the growth-promoting activity of PRL. hPRL complementary DNA was obtained from the American Type Culture Collection and subcloned into pT7-SCII after site-directed mutagenesis using the deoxyuridine approach. Proteins were expressed in Escherichia coli BL21 (DE3) and were primarily found in inclusion bodies. Agonist and antagonist activities of each serine 179 mutant were assessed using the Nb2 bioassay. Compared with standard hPRL, the recombinant wild-type was more active in the Nb2 assay, attesting to both the absence, or low level, of endotoxin contamination in preparations from these cells and the appropriate folding of the molecule. The aspartate and glutamate mutants had no intrinsic agonist activity, but both antagonized the growth-promoting activity of wild-type PRL, with the aspartate mutant proving to be a very effective antagonist. Two hundred picograms per ml of the aspartate mutant negated 75% of the growth response to 400 pg/ml wild-type PRL. When serine 179 was mutated to alanine or valine, mutant PRLs with 0% and 14% of the biological activity of wild-type PRL, respectively, were produced. These results demonstrate 1) that molecular mimicry of the phosphorylated hormone does produce a PRL antagonist, and 2) that the serine at position 179 is crucial to the growth-promoting activity of PRL. The aspartate mutant can now be used to study many aspects of the physiology of PRL.

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