Lumbar Intraspinal Spindle Cell Rhabdomyosarcoma as a Rare Cause of Spinal Stenosis: A Case Report.

Unlabelled: Rhabdomyosarcoma (RMS) represents the most common sarcoma in childhood yet is extremely rare in adults, with only a handful of cases reported. Here we present a case of intraspinal spindle cell RMS in an adult who presented as a typical case of spinal stenosis. To our knowledge, this is the first reported case of lumbar intraspinal spindle cell RMS in an adult patient.

Heterogeneous effects of calorie restriction on in vivo glucose uptake and insulin signaling of individual rat skeletal muscles.

Calorie restriction (CR) (consuming ~60% of ad libitum, AL, intake) improves whole body insulin sensitivity and enhances insulin-stimulated glucose uptake by isolated skeletal muscles. However, little is known about CR-effects on in vivo glucose uptake and insulin signaling in muscle. Accordingly, 9-month-old male AL and CR (initiated when 3-months-old) Fischer 344 x Brown Norway rats were studied using a euglycemic-hyperinsulinemic clamp with plasma insulin elevated to a similar level (~140 µU/ml) in each diet group.

Greater filamin C, GSK3α, and GSK3β serine phosphorylation in insulin-stimulated isolated skeletal muscles of calorie restricted 24 month-old rats.

Moderate calorie restriction (CR) can improve insulin-stimulated Akt phosphorylation and glucose uptake in muscles from 24 month-old rats, but the specific Akt substrates linking CR-effects on Akt to glucose uptake and other cellular processes are uncertain. We probed CR's influence on site-specific phosphorylation of five Akt substrates (AS160(Ser588), TBC1D1(Thr596), FLNc(Ser2213), GSK3α(Ser21), and GSK3β(Ser9)) in predominantly fast-twitch (epitrochlearis) and predominantly slow-twitch (soleus) muscles. We observed no CR-effect on phosphorylation of AS160(Ser588) or TBC1D1(Thr596), but there was a CR-induced increase in insulin-stimulated FLNc(Ser2213), GSK3α(Ser21), and GSK3β(Ser9) phosphorylation for both muscles.

Greater insulin-mediated Akt phosphorylation concomitant with heterogeneous effects on phosphorylation of Akt substrates in soleus of calorie-restricted rats.

Akt is a serine/threonine kinase that plays a key role in numerous cellular functions including metabolism, growth, protein synthesis, apoptosis, and cell proliferation. The most consistent and robust effect of moderate calorie restriction (CR; ~60% of ad libitum, AL, food consumption) on insulin signaling in rodent muscle has been enhanced insulin-induced phosphorylation of Akt (pAkt). However, there is limited knowledge regarding the mechanism for this enhancement and its consequences in predominantly slow-twitch muscle.

Preventing the calorie restriction-induced increase in insulin-stimulated Akt2 phosphorylation eliminates calorie restriction's effect on glucose uptake in skeletal muscle.

Calorie restriction (CR; ~60% of ad libitum, AL, consumption) improves insulin-stimulated glucose uptake in skeletal muscle. The precise cellular mechanism for this healthful outcome is unknown, but it is accompanied by enhanced insulin-stimulated activation of Akt. Previous research using Akt2-null mice demonstrated that Akt2 is essential for the full CR-effect on insulin-stimulated glucose uptake by muscle.

Calorie restriction enhances insulin-stimulated glucose uptake and Akt phosphorylation in both fast-twitch and slow-twitch skeletal muscle of 24-month-old rats.

Calorie restriction (CR) induces enhanced insulin-stimulated glucose uptake in fast-twitch (type II) muscle from old rats, but the effect of CR on slow-twitch (type I) muscle from old rats is unknown. The purpose of this study was to assess insulin-stimulated glucose uptake and phosphorylation of key insulin signaling proteins in isolated epitrochlearis (fast-twitch) and soleus (slow-twitch) muscles from 24-month-old ad libitum fed and CR (consuming 65% of ad libitum, intake) rats. Muscles were incubated with and without 1.

Mechanisms for increased insulin-stimulated Akt phosphorylation and glucose uptake in fast- and slow-twitch skeletal muscles of calorie-restricted rats.

Calorie restriction [CR; ~65% of ad libitum (AL) intake] improves insulin-stimulated glucose uptake (GU) and Akt phosphorylation in skeletal muscle. We aimed to elucidate the effects of CR on 1) processes that regulate Akt phosphorylation [insulin receptor (IR) tyrosine phosphorylation, IR substrate 1-phosphatidylinositol 3-kinase (IRS-PI3K) activity, and Akt binding to regulatory proteins (heat shock protein 90, Appl1, protein phosphatase 2A)]; 2) Akt substrate of 160-kDa (AS160) phosphorylation on key phosphorylation sites; and 3) atypical PKC (aPKC) activity. Isolated epitrochlearis (fast-twitch) and soleus (slow-twitch) muscles from AL or CR (6 mo duration) 9-mo-old male F344BN rats were incubated with 0, 1.