Proliferation and activation of human mononuclear cells induced by ionomycin and a serum free medium

NRC publication: Ye

Thrombospondin is synthesized and secreted by human osteoblasts and osteosarcoma cells. A model to study the different effects of thrombospondin in cell adhesion

Peer reviewed: YesNRC publication: Ye

Evidence that the activation of an inactive pool of membrane- associated kinase C is linked to the IL-2-dependent survival of T lymphocytes

NRC publication: Ye

Correlation between endogenous membrane PKC activity and proliferation versus differentiation of normal and HPV16 transformed rat myoblast (L 6 cells): Histochem.J.

NRC publication: Ye

Parathyroid hormone domain for protein kinase C stimulation located within amphiphilic helix

Parathyroid hormone (PTH) plays a major role in regulating circulating levels of calcium. Biological activites of this 84-residue long peptide, as well as of the equipotent 1-34 fragment, are believed to be linked to the stimulation of adenylate cyclase activity [1]. However, recent data indicate that some major functions of PTH may be mediated by an alternative mechanism that involves stimulation of membrane-associated protein kinase C (PKC) [2]. To define the domain of the hormone responsible for PKC activation, we have synthesized a series of human PTH fragments and assayed them using ROS 17/2 rat osteosarcoma cells. Biological studies with PTH fragments were complimented by conformational analysis using the methods of CD spectroscopy, secondary structure predictions, and molecular dynamics simulations.NRC publication: Ye

Intracellular calcium responses to 1% DMSO in normal and human papillomavirus type 16 (HPV16) transfected rat myoblast (L 6 cells) using imaging analysis: Histochem.J.

NRC publication: Ye

Parathyroid hormone stimulates protein kinase C but not adenylate cyclase in mouse epidermal keratinocytes: J.Cell Physiol.

NRC publication: Ye

A C-terminal fragment of parathyroid hormone-related protein, PTH-rP(107-111) stimulates membrane-associated protein kinases C's activity and modulates the proliferation of human and murine skin keratinocytes

Low concentrations of the C-terminal parathyroid hormone-related protein (PTHrP) fragments, PTHrP-(107-111) and PTHrP-(107-139), stimulated membrane-associated protein kinase Cs (PKCs), but not adenylyl cyclase or an internal Ca2+ surge, in early passage human skin keratinocytes and BALB/MK-2 murine skin keratinocytes. The fragment maximally stimulated membrane-associated PKCs in BALB/MK-2 cells at 5 x 10(-9) to 10(-8) M. The maximally PKC-stimulating concentrations of PTHrP-(107-111) also stopped or stimulated BALB/MK-2 keratinocyte proliferation depending on whether the cells were, respectively, cycling or quiescent at the time of exposure. Thus, just one brief (30-minute) pulse of 10(-8) M PTHrP-(107-111) stopped the proliferation of BALB/MK-2 keratinocytes for at least 5 days. On the other hand, daily 30-minute pulses of 10(-8) M PTHrP-(107-111) started and then maintained the proliferation of initially quiescent BALB/MK-2 cells. Similarly PTHrP-(107-111) inhibited DNA synthesis by cycling primary adult human keratinocytes, but it stimulated DNA synthesis by quiescent human keratinocytes

The protein kinase-C activation domain of the parathyroid hormone

NRC publication: Ye