Management of incisional scar is intimately connected to stages of wound healing. The management of an elective surgery patient begins with a thorough informed consent process in which the patient is made aware of personal and clinical circumstances that cannot be modified, such as age, ethnicity, and previous history of hypertrophic scars. In scar prevention, the single most important modifiable factor is wound tension during the proliferative and remodeling phases, and this is determined by the choice of incision design. Traditional incisions most often follow relaxed skin tension lines, but no such lines exist in high surface tension areas. If such incisions are unavoidable, the patient must be informed of this ahead of time. The management of a surgical incision does not end when the sutures are removed. Surgical scar care should be continued for one year. Patient participation is paramount in obtaining the optimal outcome. Postoperative visits should screen for signs of scar hypertrophy and has a dual purpose of continued patient education and reinforcement of proper care. Early intervention is a key to control hyperplastic response. Hypertrophic scars that do not improve by 6 months are keloids and should be managed aggressively with intralesional steroid injections and alternate modalities.Graphical Abstract

No abstract

Glucokinase (GK), which phosphorylates D-glucose, is a major glucose sensor in β-cells for glucose-stimulated insulin secretion (GSIS) and is a promising new drug target for type 2 diabetes (T2D). In T2D, pancreatic β-cells exhibit defective glucose sensitivity, which leads to impaired GSIS. Although glucagon-like peptide-1-(7-36)-amide (GLP-1) is known to enhance β-cell glucose sensitivity, the effect of GLP-1 on GK activity is still unknown. The present study demonstrated that GLP-1 pretreatment for 30 min significantly enhanced GK activity in a glucose-dependent manner, with a lower Michaelis-Menten constant (K(m)) but unchanged maximal velocity (V(max)). Thus, GLP-1 acutely enhanced cellular glucose uptake, mitochondrial membrane potential, and cellular ATP levels in response to glucose in rat INS-1 and native β-cells. This effect of GLP-1 occurred via its G protein-coupled receptor pathway in a cAMP-dependent but protein kinase A-independent manner with evidence of exchange protein activated by cAMP (Epac) involvement. Silencing Epac2, interacting molecule of the small G protein Rab3 (Rim2), or Ras-associated protein Rab3A (Rab3A) significantly blocked the effect of GLP-1. These results suggested that GLP-1 can further potentiate GSIS by enhancing GK activity through the signaling of Epac2 to Rim2 and Rab3A, which is the similar pathway for GLP-1 to potentiate Ca(2+)-dependent insulin granule exocytosis. The present finding may also be an important mechanism of GLP-1 for recovery of GSIS in T2D.

Therapeutic, IV.