The Impact of Emicizumab Prophylaxis on Hospitalizations and Emergency Department Visits Among Hemophilia A Patients Is Age Related.

Introduction: Hemophilia A (HA) therapy poses a significant healthcare burden. In recent years, emicizumab has been approved for prophylaxis. The current study explores the impact of transitioning to emicizumab on emergency department (ED) visits and hospitalizations in pediatric and adult HA patients.

Subcutaneous tranexamic acid in upper eyelid blepharoplasty: a prospective randomized pilot study.

Objective: Postoperative ecchymoses or hematomas can prolong healing from surgery, and a search for locally administered agents that decrease bleeding is warranted. The objective of this study is to evaluate whether preoperative subcutaneous injection of tranexamic acid (TXA) reduces intra- and postoperative bleeding or ecchymoses in skin-only upper eyelid blepharoplasty surgery.

Design: This is a prospective randomized, double-blind, controlled study.

Insulin-induced translocation of IR to the nucleus in insulin responsive cells requires a nuclear translocation sequence.

Insulin binding to its cell surface receptor (IR) activates a cascade of events leading to its biological effects. The Insulin-IR complex is rapidly internalized and then is either recycled back to the plasma membrane or sent to lysosomes for degradation. Although most of the receptor is recycled or degraded, a small amount may escape this pathway and migrate to the nucleus of the cell where it might be important in promulgation of receptor signals.

Topical Hemostatic-Anesthetic Solution to Reduce Bleeding During Mohs Micrographic Surgery: A Case Control Study.

Background: Between stages of Mohs micrographic surgery, the wound is dressed and the patient waits for the histopathological results.


Objective: To investigate the efficacy of a hemostatic-anesthetic solution-impregnated gauze in decreasing bleeding between Mohs stages.


Materials And Methods: Twenty patients were treated with a hemostatic-anesthetic solution composed of tranexamic acid, adrenaline, and lidocaine (TAL), and 20 others were treated with a saline solution for control.

Protein kinase Cδ but not PKCα is involved in insulin-induced glucose metabolism in hepatocytes.

The liver is a major insulin-responsive tissue responsible for glucose regulation. One important mechanism in this phenomenon is insulin-induced glycogen synthesis. Studies in our laboratory have shown that protein kinase Cs delta (PKCδ) and alpha (α) have important roles in insulin-induced glucose transport in skeletal muscle, and that their expression and activity are regulated by insulin.

Insulin stimulation of PKCδ triggers its rapid degradation via the ubiquitin-proteasome pathway.

Insulin rapidly upregulates protein levels of PKCδ in classical insulin target tissues skeletal muscle and liver. Insulin induces both a rapid increase in de novo synthesis of PKCδ protein. In this study we examined the possibility that insulin may also inhibit degradation of PKCδ.

Sarcopoterium spinosum extract as an antidiabetic agent: in vitro and in vivo study.

Ethnopharmacological Relevance: Sarcopoterium spinosum (L.) sp., a common plant in the Mediterranean region, is widely used as an antidiabetic drug by Bedouin healers.

The regulatory domain of protein kinase C delta positively regulates insulin receptor signaling.

Protein kinase C delta (PKCdelta) is induced by insulin to rapidly associate with insulin receptor (IR) and upregulates insulin signaling. We utilized specific JM and CT receptor domains and chimeras of PKCalpha and PKCdelta regulatory and catalytic domains to elucidate which components of PKCdelta are responsible for positive regulatory effects of PKCdelta on IR signaling. Studies were performed on L6 and L8 skeletal muscle myoblasts and myotubes.

Insulin increases nuclear protein kinase Cdelta in L6 skeletal muscle cells.

Protein kinase C (PKC) isoforms are involved in the transduction of a number of signals important for the regulation of cell growth, differentiation, apoptosis, and other cellular functions. PKC proteins reside in the cytoplasm in an inactive state translocate to various membranes to become fully activated in the presence of specific cofactors. Recent evidence indicates that PKC isoforms have an important role in the nucleus.

Cytosolic protein tyrosine phosphatase-epsilon is a negative regulator of insulin signaling in skeletal muscle.

Whereas positive regulatory events triggered by insulin binding to insulin receptor (IR) have been well documented, the mechanism by which the activated IR is returned to the basal status is not completely understood. Recently studies focused on the involvement of protein tyrosine phosphatases (PTPs) and how they might influence IR signaling. In this study, we examined the possibility that cytosolic PTPepsilon (cytPTPepsilon) is involved in IR signaling.